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A Comparative Study on the NAD Glycohydrolase of the Maternal and Neonatal Erythrocytes
Author(s) -
Suh Byung Hee,
Lee Jae Hyun,
Cho Yong Ho
Publication year - 1985
Publication title -
asia‐oceania journal of obstetrics and gynaecology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.597
H-Index - 50
eISSN - 1447-0756
pISSN - 0389-2328
DOI - 10.1111/j.1447-0756.1985.tb00729.x
Subject(s) - nad+ kinase , nicotinamide , isozyme , chemistry , haematopoiesis , band 3 , biochemistry , red blood cell , enzyme , biology , microbiology and biotechnology , erythrocyte membrane , membrane , stem cell
The subcellular localization of NADase in the ghost fraction (96%) of neonatal erythrocytes was localized more than in the maternal ghost fraction (83%). The inhibition by free nicotinamide of hydrolytic activity of NADase was found to be greater (approximately twice) in the neonatal erythrocytes than in the maternal erythrocytes. The activatory effect was exerted on the both maternal and neonatal ghost‐NADase by the addition of lower concentration (less than 0.6 M) of urea. The membraneous protein of erythrocytes was fractionated into 5 bands namely, band I, II, III, IV, V and VI in the case of maternal erythrocytes in good contrast of 7 bands for the neonatal erythrocytes namely, I, II, III, IV, V, VI and VII. From these results, it was suggested that there is a definite difference between membraneous protein of maternal and neonatal erythrocytes and NAD glycohydrolase activity and it is reasoned to be due to the independent erythropoietic site for two individuals. The erythrocytes NAD glycohydrolase might be one of the isozyme which change their properties during developmental maturation. The possible functions of erythrocytes NAD glycohydrolase were also discussed with regard to erythrocytes maturation in hematopoietic system.