The possible existence of a heat-stable alkaline proteinase (HAP) in rat skeletal muscle.
1. A unique caseinolytic activity was found in the crude extract from chicken and rat skeletal muscle. Hardly any activity was detected at physiological assay temperatures at pH 8.0 but did well at around 60 degrees C. 2. The activity partially purified from rat skeletal muscle showed optimum pH at around 8.0 at 60 degrees C. It hardly hydrolyzed casein below 50 degrees C, but in the presence of 5 M urea it showed relatively high activity at 30 degrees C. The activity was completely stable at 50 degrees C for 1 hr. 3. The activity seems to be contained in a high mol. wt (450,000) protein from the elution volume and is due to cysteine proteinase from the effect of inhibitors. 4. The above properties agreed with those of the heat-stable alkaline proteinase (HAP) of fish purified homogeneously by electrophoresis. This seems to suggest that HAP may also exist in rat skeletal muscle.
Makinodan
Y
Y
Department of Fisheries, Faculty of Agriculture, Kinki University, Higashi-Osaka, Japan.
Toyohara
H
H
Yokoyama
Y
Y
Kinoshita
M
M
D000818:Animals; D002645:Chickens; D005399:Fishes; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008297:Male; D009132:Muscles / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000032:analysis* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D010447:Peptide Hydrolases