[Structure of cytoplasmic glycerol-3-phosphate dehydrogenase in experimental atherosclerosis in rabbits].
Differences in the ratio of molecular forms of crystalline glycerol-3-phosphate dehydrogenase (GPD, EC 1.1.1.8) from sceletal muscle and in their primary structure were found in rabbits with experimental atherosclerosis as compared with normal animals. In atherosclerosis the molecular weight of GPD and of its fragments was increased; the amino acid composition of these GPD molecules differs from that of control rabbits as shown by estimation of content of 8 amino acids. Experimental atherosclerosis is apparently related to alteration in the GPD primary structure.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001161:Arteriosclerosis / Q000201:enzymology*; D003593:Cytoplasm / Q000201:enzymology*; D005993:Glycerolphosphate Dehydrogenase / Q000032:analysis*; D007525:Isoelectric Focusing; D008968:Molecular Conformation; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D011817:Rabbits; D013329:Structure-Activity Relationship
D000596:Amino Acids; D005993:Glycerolphosphate Dehydrogenase
O strukture tsitoplazmaticheskoĭ glitserol-3-fosfatdegidrogenazy pri éksperimental'nom ateroskleroze krolikov.