INVITRO NONENZYMATIC GLYCOSYLATION OF MYOFIBRILLAR PROTEINS

Authors
Citation
I. Syrovy et Z. Hodny, INVITRO NONENZYMATIC GLYCOSYLATION OF MYOFIBRILLAR PROTEINS, International Journal of Biochemistry, 25(6), 1993, pp. 941-946
Citations number
35
Categorie Soggetti
Biology
ISSN journal
0020711X
Volume
25
Issue
6
Year of publication
1993
Pages
941 - 946
Database
ISI
SICI code
0020-711X(1993)25:6<941:INGOMP>2.0.ZU;2-I
Abstract
1. Glycation is non-enzymatic modification of proteins by sugars in wh ich not only structural but also biological properties of proteins are altered. 2. Our in vitro experiments show that incubation of myofibri llar proteins with ribose results in sugar attachment to proteins and at the same time myofibrillar ATPase activity is lowered. 3. DETAPAC, aminoguanidine and 2-mercaptoethanol all partially block myofibrillar protein glycation and ATPase activity is less inactivated. 4. The depe ndence of ATPase activity of myofibrils incubated with ribose on the a mount of 2-mercaptoethanol present suggests that also modification of SH groups is involved in enzyme inactivation. 5. Electrophoretic studi es revealed that heavy chains of myosin, actin, and tropomyosins are p roteins which are mainly glycated in vitro.