[Thermal inactivation kinetics of cathepsin D from porcine muscle tissue in the presence of sodium chloride].
The effect of incubation temperature on the activity of cathepsin D from pig muscles was studied at different pH values. The highest activity of cathepsin D was observed at pH 3.0 and 37 degrees C. Heat stability of cathepsin D was studied when incubating muscle homogenates in a buffer pH 3.0 at 37 degrees, 50 degrees, 60 degrees and 70 degrees during 1 h containing sodium chloride or without it. When cathepsin D was incubated with sodium chloride it lost its activity independent of the temperature. Moreover, the higher the temperature of the process the greater the rate of cathepsin D inactivation.
Kudriashov
L S
LS
Shalakina
L P
LP
Bol'shakov
A S
AS
D000818:Animals; D002402:Cathepsin D / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D012965:Sodium Chloride / Q000494:pharmacology*; D013552:Swine
D012965:Sodium Chloride; D002402:Cathepsin D
Kinetika termoinaktivatsii katepsina D svinoì myshechnoĭ tkani v prisutstvii khlorida natria.