PLATELET GLYCOHYDROLASE ACTIVITIES - CHARACTERIZATION AND RELEASE

被引：11

作者：

EMILIANI, C ^{[1
]}

MARTINO, S ^{[1
]}

ORLACCHIO, A ^{[1
]}

VEZZA, R ^{[1
]}

NENCI, GG ^{[1
]}

GRESELE, P ^{[1
]}

机构：

[1] UNIV PERUGIA,IST MED INTERNA & MED VASC,I-06100 PERUGIA,ITALY

来源：

CELL BIOCHEMISTRY AND FUNCTION | 1995年 / 13卷 / 01期

关键词：

LYSOSOMAL GLYCOHYDROLASES; ISOENZYMES; HUMAN PLATELETS; ACTIVATION SECRETION;

D O I：

10.1002/cbf.290130108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Granules containing acid hydrolases have been detected in human platelets but have not been thoroughly characterized. We have studied the activity and characteristics of glycohydrolases present in normal human platelets, evaluated their release upon stimulation with thrombin, and assessed the contribution of platelet - released lysosomal contents to the glycohydrolase activity present in normal serum. Platelets contained a remarkable glycohydrolase activity with a prevalence of beta - N-acetylhexosaminidase. All glycohydrolases were released to some extent upon stimulation with thrombin and contributed to the glycohydrolase activity found in human serum. alpha-Mannosidase and alpha-galactosidase were partially inactivated after release by a mechanism as yet undefined. In addition, thrombin stimulation affects the intraplatelet isoenzyme pattern of beta-N-acetylhexosaminidase by producing the appearance of a new form.

引用

页码：31 / 39

页数：9

共 23 条

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