{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T19:41:48Z","timestamp":1778528508744,"version":"3.51.4"},"reference-count":15,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,9,5]],"date-time":"2008-09-05T00:00:00Z","timestamp":1220572800000},"content-version":"vor","delay-in-days":2439,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Progress"],"published-print":{"date-parts":[[2002,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Glycomacropeptide (GMP) found in sweet whey is a biologically active compound released from \u03ba\u2010casein by the action of chymosin during cheese making. This study was undertaken to purify GMP from sweet whey as a research chemical on a laboratory scale. Glycomacropeptide was isolated from proteins and other non\u2010GMP compounds by deproteinization with trichloroacetic acid and gel chromatography on Sephacryl S\u2010200. The purified GMP accounted for 0.12% of dry sweet whey powder and contained 107.0, 50.9, 61.2 and 4.3 \u03bcg, respectively, of sialic acid, galactose, galactosamine and phosphorus per mg dry weight. The GMP was of high purity, with its amino acid composition showing undetectable levels of phenylalanine, tyrosine and arginine, the amino acids that do not occur in bovine GMP. On gel electrophoresis, the GMP showed a single broad band with an average mobility faster than that of carbonic anhydrase (molecular weight = 31 kDa). The purified GMP may be used as a standard glycopeptide in chromatography and electrophoresis and may also be used to test various known or unknown properties and biological activities of this compound.<\/jats:p>","DOI":"10.1021\/bp010195u","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T02:08:28Z","timestamp":1027649308000},"page":"409-412","source":"Crossref","is-referenced-by-count":24,"title":["Purification of \u03ba\u2010Casien Glycomacropeptide from Sweet Whey with Undetectable Level of Phenylalanine"],"prefix":"10.1002","volume":"18","author":[{"given":"Takuo","family":"Nakano","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eryck","family":"R. Silva\u2010Hernandez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noriaki","family":"Ikawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lech","family":"Ozimek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,9,5]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.3168\/jds.S0022-0302(84)81485-X"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1017\/S0007114500002233"},{"key":"e_1_2_6_4_2","unstructured":"Ayers J. S.;Coolbear K. P.;Elgar D. F.Process for isolating glycomacropeptide from dairy products with a phenylalanine impurity of 0.5% w\/w. PCT\/WO 98\/14071 1998."},{"key":"e_1_2_6_5_2","unstructured":"Etzel M. R.Production of \u03ba\u2010casein macropeptide. PCT\/WO 99\/18808 1999."},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1005618619167"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1005649415447"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00833026"},{"key":"e_1_2_6_9_2","doi-asserted-by":"crossref","first-page":"3201","DOI":"10.1128\/iai.56.12.3201-3208.1988","article-title":"Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives","volume":"56","author":"Neeser J.","year":"1988","journal-title":"Infect. Immun."},{"key":"e_1_2_6_10_2","first-page":"171","article-title":"Detection of rennet whey solids in skim milk powder and buttermilk powder with reversed\u2010phase HPLC","volume":"43","author":"Olieman C.","year":"1989","journal-title":"Neth. Milk Dairy J."},{"key":"e_1_2_6_11_2","first-page":"629","article-title":"Gel chromatography of glycomacropeptide (GMP) from sweet whey on Sephacryl S\u2010200 at different pH's and on Sephadex G\u201075 in 6 M guanidine hydrochloride","volume":"53","author":"Nakano T.","year":"1998","journal-title":"Milchwissenschaft"},{"key":"e_1_2_6_12_2","first-page":"153","article-title":"A rapid and sensitive high\u2010performance liquid chromatography method of following the action of chymosin in milk","volume":"36","author":"van Hooydonk A. C. M.","year":"1982","journal-title":"Neth. Milk Dairy J"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1021\/jf981077y"},{"key":"e_1_2_6_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0958-6946(97)00062-9"},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2400087"},{"key":"e_1_2_6_16_2","first-page":"688","article-title":"Determination of \u03ba casein glycomacropeptide by high performance liquid chromatography without trichloroacetic acid pretreatment","volume":"47","author":"Kawakami H.","year":"1992","journal-title":"Milchwissenschaft"}],"container-title":["Biotechnology Progress"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1021%2Fbp010195u","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/aiche.onlinelibrary.wiley.com\/doi\/pdf\/10.1021\/bp010195u","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T08:54:27Z","timestamp":1761641667000},"score":1,"resource":{"primary":{"URL":"https:\/\/aiche.onlinelibrary.wiley.com\/doi\/10.1021\/bp010195u"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,1]]},"references-count":15,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2002,1]]}},"alternative-id":["10.1021\/bp010195u"],"URL":"https:\/\/doi.org\/10.1021\/bp010195u","archive":["Portico"],"relation":{},"ISSN":["8756-7938","1520-6033"],"issn-type":[{"value":"8756-7938","type":"print"},{"value":"1520-6033","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,1]]}}}