{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T21:32:42Z","timestamp":1790803962256,"version":"4.1.0"},"reference-count":80,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[1971,6,1]],"date-time":"1971-06-01T00:00:00Z","timestamp":44582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The American Journal of Clinical Nutrition"],"published-print":{"date-parts":[[1971,6]]},"DOI":"10.1093\/ajcn\/24.6.642","type":"journal-article","created":{"date-parts":[[2018,1,23]],"date-time":"2018-01-23T09:53:26Z","timestamp":1516701206000},"page":"642-650","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":24,"title":["Hexokinase: a compartmented enzyme"],"prefix":"10.1016","volume":"24","author":[{"given":"James W.","family":"Anderson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert H.","family":"Herman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J.B.","family":"Tyrrell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert M.","family":"Cohn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1093\/ajcn\/24.6.642_bib1","first-page":"176","article-title":"Ueber die enzymatische Milchs\u00e4urebildung im Muskelextrakt; die Milchs\u00e4urebildung aus den g\u00e4rf\u00e4higen Hexosen.","volume":"183","author":"MEYERHOF","year":"1927","journal-title":"Biochem. Z."},{"key":"10.1093\/ajcn\/24.6.642_bib2","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1007\/BF01491989","article-title":"\u00dcber die Wirkungsweise derHexokinase.","volume":"23","author":"MEYERHOF","year":"1935","journal-title":"Naturwissenschaften"},{"key":"10.1093\/ajcn\/24.6.642_bib3","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0021-9258(18)72324-7","article-title":"The role of myokinase in trans-phosphorylations; the enzymatic phosphorylation of hexoses by adenyl pyrophosphate.","volume":"148","author":"COLOWICK","year":"1943","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib4","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1085\/jgp.29.6.379","article-title":"Isolation of hexokinase from Baker\u2019s yeast.","volume":"29","author":"BERGER","year":"1946","journal-title":"J. Gen. Physiol."},{"key":"10.1093\/ajcn\/24.6.642_bib5","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1085\/jgp.29.6.393","article-title":"Crystalline hexokinase (heterophosphatase): method of isolation and properties","volume":"29","author":"KUNITZ","year":"1946","journal-title":"J. Gen. Physiol."},{"key":"10.1093\/ajcn\/24.6.642_bib6","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/0006-291X(70)90755-2","article-title":"The molecular weight of the undegraded polypeptide chain of yeast hexokinase.","volume":"39","author":"PRINGLE","year":"1970","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib7","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1042\/bj0490339","article-title":"Studies on hexokinase. I. The hexokinase activity of rat-brain extracts.","volume":"49","author":"WEIL-MALHERBE","year":"1951","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib8","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1016\/S0021-9258(18)56270-0","article-title":"A comparative study of hexokinase from yeast and animal tissues.","volume":"186","author":"SLEIN","year":"1950","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib9","doi-asserted-by":"crossref","first-page":"2542","DOI":"10.1016\/S0021-9258(19)76910-5","article-title":"Hepatic glucokinase in the fed, fasted, and alloxandiabetic rat.","volume":"235","author":"DIPIETRO","year":"1960","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(18)81278-9","article-title":"Glucokinase and hexokinase in liver in relation to glycogen synthesis.","author":"VI\u00d1UELA","year":"1963","journal-title":"J, Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib11","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0006-3002(63)90494-3","article-title":"On the presence of two soluble glucose-phosphorylating enzymes in adult liver and the development of one of these after birth.","volume":"77","author":"WALKER","year":"1963","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib12","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/0006-291X(64)90038-5","article-title":"Multiple molecular forms of ATP: hexose-6-phosphotransferase from rat liver.","volume":"16","author":"GONZ\u00c1LEZ","year":"1964","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib13","doi-asserted-by":"crossref","first-page":"1218","DOI":"10.1073\/pnas.54.4.1218","article-title":"Multiple forms of hexokinase in the rat: tissue distribution, age dependency, and properties.","volume":"54","author":"KATZEN","year":"1965","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1093\/ajcn\/24.6.642_bib14","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/0006-291X(66)90352-4","article-title":"The effect of diabetes and insulin in vivo and in vitro on a low Km form of hexokinase from various rat tissues.","volume":"24","author":"KATZEN","year":"1966","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib15","doi-asserted-by":"crossref","first-page":"3546","DOI":"10.1016\/S0021-9258(18)99866-2","article-title":"Multiple hexokinases of rat tissues.","volume":"241","author":"GROSSBARD","year":"1966","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib16","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/0065-2571(67)90025-8","article-title":"The multiple forms of mammalian hexokinase and their significance to the action of insulin.","volume":"5","author":"KATZEN","year":"1967","journal-title":"Advan. Enzyme Regul."},{"key":"10.1093\/ajcn\/24.6.642_bib17","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1111\/j.1749-6632.1968.tb11899.x","article-title":"Studies on isozymes of hexokinase in animal tissues.","volume":"151","author":"SCHIMKE","year":"1968","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1093\/ajcn\/24.6.642_bib18","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1042\/bj0770610","article-title":"The intracellular distribution of glycolytic and other enzymes in rat-brain homogenates and mitochondrial preparations.","volume":"77","author":"JOHNSON","year":"1960","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib19","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1016\/S0021-9258(18)96139-9","article-title":"Mitochondrial hexokinase: release, rebinding, and location.","volume":"242","author":"ROSE","year":"1967","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib20","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1042\/bj1010048","article-title":"Glucose metabolism in the mucosa of the small intestine: enzymes of the pentose phosphate pathway.","volume":"101","author":"SRIVASTAVA","year":"1966","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib21","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0021-9258(17)41536-5","article-title":"Anaerobic glycolysis in nervous tissue.","volume":"161","author":"UTTER","year":"1946","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib22","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/S0021-9258(19)52639-4","article-title":"The association of hexokinase with particulate fractions of brain and other tissue homogenates.","volume":"203","author":"CRANE","year":"1953","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib23","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1471-4159.1959.tb13328.x","article-title":"Glycolytic activity associated with rat brain mitochondria.","volume":"5","author":"BALAZS","year":"1959","journal-title":"J. Neurochem."},{"key":"10.1093\/ajcn\/24.6.642_bib24","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S0021-9258(18)98178-0","article-title":"Glycolytic and oxidative phosphorylative studies with intact and disrupted rat brain mitochondria.","volume":"234","author":"ABOOD","year":"1959","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib25","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1111\/j.1471-4159.1963.tb05054.x","article-title":"Isolation from rat brain of mitochondria devoid of glycolytic activity.","volume":"10","author":"TANAKA","year":"1963","journal-title":"J. Neurochem."},{"key":"10.1093\/ajcn\/24.6.642_bib26","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1016\/S0021-9258(19)34187-0","article-title":"Brain hexokinase: a proposed relation between soluble-particulate distribution and activity","volume":"243","author":"WILSON","year":"1968","journal-title":"in vivo. J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib27","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/0006-291X(69)90698-6","article-title":"Sequential control of hexokinase in ascites cells.","volume":"35","author":"GUMAA","year":"1969","journal-title":"Biochem, Biophys. Res, Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib28","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/0006-291X(70)91085-5","article-title":"Hexokinase binding sites on mitochondrial membranes.","volume":"38","author":"KROPP","year":"1970","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib29","first-page":"4081","article-title":"Multiple forms of hexokinases: activities associated with subcellular particle and soluble fractions of normal and streptozotocin diabetic rat tissue.","volume":"245","author":"KATZER","year":"1970","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib30","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1021\/bi00837a007","article-title":"Brain hexokinase. The preparation of inner and outer mitochondrial membranes.","volume":"8","author":"CRAVEN","year":"1969","journal-title":"Biochemistry"},{"key":"10.1093\/ajcn\/24.6.642_bib31","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1042\/bj1180025","article-title":"Cerebral-cortex hexokinase: comparison of properties of solubilized mitochondrial and cytoplasmic activities.","volume":"118","author":"THOMPSON","year":"1970","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib32","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/0304-4165(70)90172-8","article-title":"The intracellular distribution of the latent hexokinase in brain.","volume":"201","author":"BIERER","year":"1970","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib33","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0003-9861(66)90176-7","article-title":"Association of heart-hexokinase with subcellular structure.","volume":"113","author":"HERNandEZ","year":"1966","journal-title":"Arch, Biochem. Biophys."},{"key":"10.1093\/ajcn\/24.6.642_bib34","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1042\/bj1090035","article-title":"Glucose metabolism in the mucosa of the small intestine. A study of hexokinase activity.","volume":"109","author":"SRIVASTAVA","year":"1969","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib35","first-page":"376","article-title":"Regulation of hexokinase activity in intestinal mucosa of alloxan-diabetic rats.","volume":"19","author":"ANDERSON","year":"1970","journal-title":"Diabetes"},{"key":"10.1093\/ajcn\/24.6.642_bib36","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1016\/S0021-9258(18)95893-X","article-title":"Soluble and particulate hexokinase of frog skeletal muscle.","volume":"242","author":"KARPATKIN","year":"1967","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib37","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/0006-291X(69)90894-8","article-title":"The effect of oestrogen on the activity and binding of multiple forms of hexokinase in the rat uterus.","volume":"37","author":"BAQUER","year":"1969","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib38","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0005-2744(68)90208-8","article-title":"Association of epididymal adipose tissue hexokinase with subcellular structures","volume":"167","author":"SPYDEVOLD","year":"1968","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib39","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/bj1090737","article-title":"The effect of anti-insulin serum and alloxan-diabetes on the distribution and multiple forms of hexokinase in lactating rat mammary gland.","volume":"109","author":"WALTERS","year":"1968","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib40","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1139\/y56-025","article-title":"The metabolism of the erythrocyte. XIII. Enzyme activity in the reticulocyte.","volume":"34","author":"RUBINSTEIN","year":"1956","journal-title":"Canad. J. Biochem. Physiol."},{"key":"10.1093\/ajcn\/24.6.642_bib41","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1146\/annurev.bi.37.070168.002043","article-title":"The catalytic and regulatory properties of enzymes","volume":"37","author":"KOSHLAND","year":"1968","journal-title":"Ann. Rev. Biochem."},{"key":"10.1093\/ajcn\/24.6.642_bib42","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1038\/225333a0","article-title":"Three-dimensional structure of adenosine triphosphate.","volume":"225","author":"KENNARD","year":"1970","journal-title":"Nature"},{"key":"10.1093\/ajcn\/24.6.642_bib43","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1042\/bj1000739","article-title":"Kinetic studies with skeletal-muscle hexokinase.","volume":"100","author":"TOEWS","year":"1966","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib44","first-page":"33","article-title":"The nature and function of hexokinase in animal tissues.","volume":"2","author":"WALKER","year":"1966","journal-title":"Essays Biochem."},{"key":"10.1093\/ajcn\/24.6.642_bib45","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1507\/endocrj1954.16.433","article-title":"Reaction mechanism of hexokinase isozymes and their insulin response.","volume":"16","author":"MACHIYA","year":"1969","journal-title":"Endocrinol. Japon."},{"key":"10.1093\/ajcn\/24.6.642_bib46","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1111\/j.1432-1033.1969.tb19620.x","article-title":"Comments on the kinetics and mechanism of yeast hexokinase action: is the binding sequence of substrates to the enzyme ordered or random?","volume":"7","author":"FROMM","year":"1969","journal-title":"European J. Biochem."},{"key":"10.1093\/ajcn\/24.6.642_bib47","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1042\/bj1050473","article-title":"Further properties and possible mechanism of action of adenosine-5'-triphosphate-D-glucose 6-phosphotransferase from rat liver.","volume":"105","author":"PARRY","year":"1967","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib48","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/S0021-9258(18)63439-8","article-title":"Product inhibition of the hexokinases","volume":"245","author":"Kosow","year":"1970","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib49","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/0006-291X(68)90291-X","article-title":"Kinetic studies of solubilized brain hexokinase with D-fructose as a substrate.","volume":"32","author":"FROMM","year":"1968","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib50","doi-asserted-by":"crossref","first-page":"3840","DOI":"10.1016\/S0021-9258(17)36426-8","article-title":"Studies on the kinetic mechanism and allosteric nature of bovine brain hexokinase.","volume":"244","author":"NING","year":"1969","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib51","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1016\/S0021-9258(19)34185-7","article-title":"Ascites tumor mitochondrial hexokinase. II. Effects of binding on kinetic properties","volume":"243","author":"Kosow,","year":"1968","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib52","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0926-6569(63)90211-6","article-title":"The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations","volume":"67","author":"CLELAND","year":"1963","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib53","doi-asserted-by":"crossref","first-page":"3503","DOI":"10.1021\/bi00863a023","article-title":"Kinetic studies of the brain hexokinase reaction. A reinvestigation with solubilized bovine enzyme.","volume":"6","author":"COPLEY","year":"1967","journal-title":"Biochemistry"},{"key":"10.1093\/ajcn\/24.6.642_bib54","series-title":"The Enzymes (2nd ed.)","first-page":"3","article-title":"Phosphoryl group transfer (survey).","author":"NORDLIE","year":"1962"},{"key":"10.1093\/ajcn\/24.6.642_bib55","series-title":"The Enzymes (2nd ed.)","first-page":"47","article-title":"Hexokinase and pentokinases.","author":"CRANE","year":"1962"},{"key":"10.1093\/ajcn\/24.6.642_bib56","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1111\/j.1432-1033.1970.tb00937.x","article-title":"Kinetic study of yeast hexokinase: inhibition of the reaction by magnesium and ATP.","volume":"13","author":"NOAT","year":"1970","journal-title":"European J. Biochem."},{"key":"10.1093\/ajcn\/24.6.642_bib57","doi-asserted-by":"crossref","first-page":"6420","DOI":"10.1016\/S0021-9258(18)63481-7","article-title":"Studies on heart phosphofructokinase: binding of native enzyme and of enzyme desensitized to allosteric control.","volume":"244","author":"LORENSON","year":"1969","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib58","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/0005-2744(71)90067-2","article-title":"Phosphofructokinase in rat jejunal mucosa: subcellular distribution, isolation and characterization","volume":"227","author":"Ho","year":"1971","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib59","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1042\/bj0870526","article-title":"The inhibition of hexokinase by disulfides.","volume":"87","author":"NESBAKKEN","year":"1963","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib60","series-title":"Ciba Found. Symp. Regulation Cell Metab.","first-page":"17","article-title":"On the meaning of intracellular structure for metabolic regulation.","author":"SIEKEVITZ","year":"1959"},{"key":"10.1093\/ajcn\/24.6.642_bib61","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/0014-4827(63)90189-7","article-title":"A morphological and biochemical study on the regulation of carbohydrate metabolism in the muscle cell","volume":"32","author":"MARGRETH","year":"1963","journal-title":"Exptl. Cell Res."},{"key":"10.1093\/ajcn\/24.6.642_bib62","article-title":"Physiological functions of the mitochondrial-bound hexokinase of ascites tumor cells.","author":"LI","year":"1966","journal-title":"Chem. Abstr."},{"key":"10.1093\/ajcn\/24.6.642_bib63","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1016\/0006-291X(70)90353-0","article-title":"Transient isolation of the hexokinase reaction from the glycolytic sequence on initiation of glycolysis in ascites tumor cells.","volume":"38","author":"COE","year":"1970","journal-title":"Biochem. Biophys. Res. Comm."},{"key":"10.1093\/ajcn\/24.6.642_bib64","series-title":"Carbohydrate Metabolism and Its Disorders","first-page":"53","article-title":"Phosphorylation and glycolysis.","author":"SOLS","year":"1968"},{"key":"10.1093\/ajcn\/24.6.642_bib65","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1093\/ajcn\/22.9.1204","article-title":"Glucose-6-phosphatase: a multifunctional enzyme.","volume":"22","author":"COHN","year":"1969","journal-title":"Am. J. Clin. Nutr."},{"key":"10.1093\/ajcn\/24.6.642_bib66","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1111\/j.1749-6632.1969.tb46428.x","article-title":"Some properties and possible physiological functions of phosphotransferase activities of microsomal glucose-6-phosphatase.","volume":"166","author":"NORDLIE","year":"1969","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1093\/ajcn\/24.6.642_bib67","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1016\/S0021-9258(18)69727-3","article-title":"TWO identical Embdem-Meyerhof enzyme systems in normal rat diaphragms differing in cytological location and response to insulin.","volume":"234","author":"SHAW","year":"1959","journal-title":"J. Biol. Chem."},{"key":"10.1093\/ajcn\/24.6.642_bib68","first-page":"835","article-title":"Insulin responsive and nonresponsive pools of glucose 6-phosphate in diaphragmatic muscle.","volume":"25","author":"SIMS","year":"1966","journal-title":"Federation Proc."},{"key":"10.1093\/ajcn\/24.6.642_bib69","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1007\/BF01897567","article-title":"Glucose-6-phosphate pools in isolated rat diaphragm.","volume":"25","author":"D\u2019AGNOLO","year":"1969","journal-title":"Experientia"},{"key":"10.1093\/ajcn\/24.6.642_bib70","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1093\/ajcn\/20.11.1242","article-title":"Intracellular glucose 6-phosphate compartmentation and glycogen synthesis.","volume":"20","author":"ZAKIM","year":"1967","journal-title":"Am. J. Clin. Nutr."},{"key":"10.1093\/ajcn\/24.6.642_bib71","first-page":"1","article-title":"Insulin and the regulation of hepatic biosynthetic activity.","volume":"24","author":"STEINER","year":"1966","journal-title":"Vitamins Hormones"},{"key":"10.1093\/ajcn\/24.6.642_bib72","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/0304-4165(70)90297-7","article-title":"The influence of alloxan-diabetes and fasting on glycolytic and gluconeogenic enzyme activities of rat intestinal mucosa and liver.","volume":"201","author":"ANDERSON","year":"1970","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib73","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/0304-4165(68)90001-9","article-title":"Dietary regulation of glycolytic enzymes. I. Adaptive changes in rat jejunum.","volume":"170","author":"STIFEL","year":"1968","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib74","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/0304-4165(68)90002-0","article-title":"The dietary regulation of the glycolytic enzymes. II. Adaptive changes in human jejunum.","volume":"170","author":"ROSENSWEIG","year":"1968","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1093\/ajcn\/24.6.642_bib75","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1042\/bj1110063","article-title":"Glucose metabolism in the mucosa of the small intestine: the effect of glucose on hexokinase activity.","volume":"111","author":"SHAKESPEARE","year":"1969","journal-title":"Biochem. J."},{"key":"10.1093\/ajcn\/24.6.642_bib76","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/0002-9343(66)90155-0","article-title":"A molecular basis for the mechanism of insulin action.","volume":"40","author":"BESSMAN","year":"1966","journal-title":"Am. J. Med."},{"key":"10.1093\/ajcn\/24.6.642_bib77","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1007\/BF01212218","article-title":"The effects of insulin and glucose on mitochondrial-bound hexokinase activity of rat epididymal adipose tissue.","volume":"5","author":"BORREBAEK","year":"1969","journal-title":"Diabetologia"},{"key":"10.1093\/ajcn\/24.6.642_bib78","first-page":"383","article-title":"Biochemische Defekte in den Blutzellen bei familiarer Panmyelopathie (TypFanconi).","volume":"1","author":"L\u00d6HR","year":"1965","journal-title":"Humangenetik"},{"key":"10.1093\/ajcn\/24.6.642_bib79","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1056\/NEJM196701052760101","article-title":"Hereditary hemolytic anemia with hexokinase deficiency. Role of hexokinase in erythrocyte aging.","volume":"276","author":"VALENTINE","year":"1967","journal-title":"New Engl. J. Med."},{"key":"10.1093\/ajcn\/24.6.642_bib80","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1172\/JCI106165","article-title":"Hemolytic anemia with impaired hexokinase activity.","volume":"48","author":"KEITT","year":"1969","journal-title":"J. Clin. Invest."}],"container-title":["The American Journal of Clinical Nutrition"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000291652332817X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000291652332817X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/academic.oup.com\/ajcn\/article-pdf\/24\/6\/642\/24186773\/642.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,31]],"date-time":"2023-10-31T12:32:24Z","timestamp":1698755544000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S000291652332817X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1971,6]]},"references-count":80,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1971,6]]}},"alternative-id":["S000291652332817X"],"URL":"https:\/\/doi.org\/10.1093\/ajcn\/24.6.642","relation":{},"ISSN":["0002-9165"],"issn-type":[{"value":"0002-9165","type":"print"}],"subject":[],"published":{"date-parts":[[1971,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hexokinase: a compartmented enzyme","name":"articletitle","label":"Article Title"},{"value":"The American Journal of Clinical Nutrition","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1093\/ajcn\/24.6.642","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 1971 American Society for Nutrition. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}