PROPERTIES OF ADP-DEGRADING ACTIVITY OF HUMAN PLACENTAL SYNCYTIOTROPHOBLAST BRUSH-BORDER MEMBRANE-VESICLES

被引:2
作者
IIOKA, H
AKADA, S
SAKAMOTO, Y
SHIMAMOTO, T
YAMADA, Y
MORIYAMA, IS
ICHIJO, M
机构
[1] Department of Obstetrics and Gynecology, Nara Medical University, Nova
关键词
D O I
10.1016/S0143-4004(05)80431-X
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The enzymatic properties of ADP (adenosine diphosphate) degradation in human placental syncytiotrophoblast brush border membrane vesicles (BBMV) were explored and the following results were obtained. BBMV had high ADP degrading activity compared to homogenate of placental villi. ADP degrading activity of BBMV; 1.05±0.05 μmol/mg protein/ min placental villi was 21 times higher than that of homogenate of placental villi. Hydrolysis of ADP by BBMV follows Michaelis-Menten saturation kinetics with an apparent Km of 10.9±0.8 μm and Vmax of 2.10±0.17 μmol/mg protein/min. The enzyme has a divalent cation requirement. EDTA (2 mm) was found to abolish ADP degrading activity but this could be restored by the addition of either magnesium or calcium ions. Maximum enzyme activity of ADP degradation in BBMV was observed at a pH close to 8.0. The enzyme was insensitive to vanadate, levamisole, oligomycin, ouabain and N-ethylmaleimide (NEM), omeprazole and adenosine (5′) pentaphospho (5′) adenosine. © 1993, Baillière Tindall. All rights reserved.
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页码:333 / 339
页数:7
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