[Comparative study of D-glyceraldehyde-3-phosphate dehydrogenase from frog and pike skeletal muscles].
The purified preparations of glyceraldehyde-3-phosphate dehydrogenase isolated from frog and pike skeletal muscles were found homogenous under polyacrylamide gel electrophoresis. Their amino acid composition is similar to that of glyceraldehyde-3-phosphate dehydrogenase from other animal species. The interaction kinetics for frog and pike glyceraldehyde-3-phosphate dehydrogenase SH-groups with 5,5'-dithio-bis-(2-nitrobenzoate) (DTNB) were studied. A negative correlation between the thermal stability of the enzyme preparations from pig, pike, lamprey and frog muscles and the reactivity of their SH-groups with respect to DTNB was observed. NAD at saturating concentrations was found to protect the enzyme from lower vertebrates muscles against thermal inactivation in a lesser degree than does the pig muscle enzyme. The weaker protective effect of NAD was observed for lamprey and frog enzyme preparations, which are characterized by a low SH-group reaction ability. Frog and pike apoenzymes are considerably more resistant to trypsin proteolysis than the pig apoenzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001001:Anura; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D004355:Drug Stability; D005399:Fishes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D007700:Kinetics; D007798:Lampreys; D009132:Muscles / Q000201:enzymology*; D011896:Rana temporaria; D013045:Species Specificity; D013552:Swine
D000596:Amino Acids; D004228:Dithionitrobenzoic Acid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
Sravnitel'noe izuchenie svoĭstv D-glitseral'degid-3-fosfatdegidrogenaz iz skeletnykh myshts liagushki i shchuki.