{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T19:33:17Z","timestamp":1779910397887,"version":"3.53.1"},"reference-count":12,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"3758","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1967,1,6]]},"abstract":"<jats:p>\n            Glucose-6-phosphate dehydrogenase in erythrocytes of the Negro type associated with enzyme deficiency (A\n            <jats:sup>-<\/jats:sup>\n            ) was separated by chromatography on a carboxymethyl-Sephadex column from the electrophoretically indistinguishable Negro variant with normal enzyme activity (A\n            <jats:sup>+<\/jats:sup>\n            ). Quantitative immunologic neutralization tests indicated that the A\n            <jats:sup>-<\/jats:sup>\n            enzyme had about the same enzymatic and serological activity as the A\n            <jats:sup>+<\/jats:sup>\n            and the normal (B\n            <jats:sup>+<\/jats:sup>\n            ) enzymes. The enzyme activity of the A\n            <jats:sup>-<\/jats:sup>\n            variant in young erythrocytes was similar to that in young cells from normal individuals, although the activity of the A\n            <jats:sup>-<\/jats:sup>\n            variant in unfractionated red cells was 10 to 15 percent of normal. These data indicate that the basic defect in the variant enzyme (A\n            <jats:sup>-<\/jats:sup>\n            ) is a structural mutation which causes more rapid degradation of the enzyme during erythrocyte aging.\n          <\/jats:p>","DOI":"10.1126\/science.155.3758.97","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T11:08:12Z","timestamp":1160046492000},"page":"97-99","source":"Crossref","is-referenced-by-count":68,"title":["Negro Variant of Glucose-6-Phosphate Dehydrogenase Deficiency (A\n            <sup>-<\/sup>\n            ) in Man"],"prefix":"10.1126","volume":"155","author":[{"given":"Akira","family":"Yoshida","sequence":"first","affiliation":[{"name":"George Stamatoyannopoulos"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arno G.","family":"Motulsky","sequence":"additional","affiliation":[{"name":"Division of Medical Genetics, Department of Medicine, University of Washington, Seattle"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","first-page":"1868","volume":"48","year":"1962","unstructured":"BOYER, S.H., ELECTROPHORETIC HETEROGENEITY OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE AND ITS RELATIONSHIP TO ENZYME DEFICIENCY IN MAN, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 48: 1868 (1962).","journal-title":"PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"},{"key":"e_1_2_1_2_1","first-page":"29","volume":"2","year":"1966","unstructured":"BROK, F, ISRAEL JOURNAL OF MEDICAL SCIENCES 2: 29 (1966).","journal-title":"ISRAEL JOURNAL OF MEDICAL SCIENCES"},{"key":"e_1_2_1_3_1","first-page":"668","volume":"64","year":"1964","unstructured":"DANON, D, DETERMINATION OF DENSITY DISTRIBUTION OF RED CELL POPULATION, JOURNAL OF LABORATORY AND CLINICAL MEDICINE 64: 668 (1964).","journal-title":"JOURNAL OF LABORATORY AND CLINICAL MEDICINE"},{"key":"e_1_2_1_4_1","first-page":"241","volume":"15","year":"1963","unstructured":"KIRKMAN, H.N., SEX-LINKED ELECTROPHORETIC DIFFERENCE IN GLUCOSE-6-PHOSPHATE DEHYDROGENASE, AMERICAN JOURNAL OF HUMAN GENETICS 15: 241 (1963).","journal-title":"AMERICAN JOURNAL OF HUMAN GENETICS"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1038\/197286a0","volume":"197","year":"1963","unstructured":"KIRKMAN, H.N., MOLECULAR DEFICIENCY OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE IN PRIMAQUINE SENSITIVITY, NATURE 197: 286 (1963).","journal-title":"NATURE"},{"key":"e_1_2_1_6_1","first-page":"938","volume":"46","year":"1960","unstructured":"KIRKMAN, H.N., DIFFERENT ENZYMIC EXPRESSIONS OF MUTANTS OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 46: 938 (1960).","journal-title":"PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/0006-291X(65)90520-6","volume":"21","year":"1965","unstructured":"LUZZATTO, L, DIFFERENT PROPERTIES OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM HUMAN ERYTHROCYTES WITH NORMAL AND ABNORMAL ENZYME LEVELS, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 21: 547 (1965).","journal-title":"BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1111\/j.1749-6632.1963.tb53743.x","volume":"103","year":"1963","unstructured":"MARKS, P.A., .4. INTERACTION OF ENZYME, COENZYME, AND SUBSTRATE WITH ANTIBODY - MULTIPLE FORMS OF ENZYMES - HUMAN GLUCOSE-6-P DEHYDROGENASE - STUDIES ON RELATION BETWEEN ANTIGENICITY AND CATALYTIC ACTIVITY - ROLE OF TPN, ANNALS OF THE NEW YORK ACADEMY OF SCIENCES 103: 902 (1963).","journal-title":"ANNALS OF THE NEW YORK ACADEMY OF SCIENCES"},{"key":"e_1_2_1_9_1","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/S0021-9258(18)64418-7","volume":"236","year":"1961","unstructured":"MARKS, P.A., ERYTHROCYTE GLUCOSE 6-PHOSPHATE DEHYDROGENASE OF NORMAL AND MUTANT HUMAN SUBJECTS - PROPERTIES OF PURIFIED ENZYMES, JOURNAL OF BIOLOGICAL CHEMISTRY 236: 10 (1961).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_10_1","first-page":"1266","volume":"183","year":"1959","unstructured":"MARKS, P.A., GENE ACTION IN ERYTHROCYTE DEFICIENCY OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE - TISSUE ENZYME-LEVELS, NATURE 183: 1266 (1959).","journal-title":"NATURE"},{"key":"e_1_2_1_11_1","first-page":"529","volume":"44","year":"1958","unstructured":"MARKS, P.A., EFFECT OF AGE ON THE ENZYME ACTIVITY IN ERYTHROCYTES, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 44: 529 (1958).","journal-title":"PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"},{"key":"e_1_2_1_12_1","doi-asserted-by":"crossref","first-page":"4966","DOI":"10.1016\/S0021-9258(18)99658-4","volume":"241","year":"1966","unstructured":"YOSHIDA, A, GLUCOSE 6-PHOSPHATE DEHYDROGENASE OF HUMAN ERYTHROCYTES .I. PURIFICATION AND CHARACTERIZATION OF NORMAL (B+) ENZYME, JOURNAL OF BIOLOGICAL CHEMISTRY 241: 4966 (1966).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"}],"container-title":["Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/science.155.3758.97","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,11]],"date-time":"2024-01-11T09:53:59Z","timestamp":1704966839000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/science.155.3758.97"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1967,1,6]]},"references-count":12,"journal-issue":{"issue":"3758","published-print":{"date-parts":[[1967,1,6]]}},"alternative-id":["10.1126\/science.155.3758.97"],"URL":"https:\/\/doi.org\/10.1126\/science.155.3758.97","relation":{},"ISSN":["0036-8075","1095-9203"],"issn-type":[{"value":"0036-8075","type":"print"},{"value":"1095-9203","type":"electronic"}],"subject":[],"published":{"date-parts":[[1967,1,6]]}}}