نتایج جستجو برای: proteinase activity

تعداد نتایج: 1142352  

2003
STUART D. ELLIOTT VINCENT P. DOLE

In a previous report (1) it was shown that, under suitable conditions, some strains of group A streptococci produce in broth cultures an extracellular proteolytic enzyme. In certain respects the enzyme resembles papain and the cathepsins in that it achieves maximal activity under reducing conditions and is inactivated by iodoacetic acid. In broth cultures the reducing conditions necessary for t...

Journal: :Zeitschrift fur Naturforschung. Section C, Biosciences 1978
N R Rauber K D Jany G Pfleiderer

The digestion of ribonuclease A by proteinase K yielded one major degradation product only, which could not be distinguished from ribonuclease S by electrophoretical and immunological methods. This component (ribonuclease K) possessing full catalytic activity was characterized to be (1--20/21--124) ribonuclease A. Combined action of proteinase K and trypsin on ribonuclease A leads to a signific...

Journal: :Insect biochemistry and molecular biology 2000
S E Wilhite T C Elden J Brzin A C Smigocki

Proteolytic activities in alfalfa weevil (Hypera postica) larval midguts have been characterized. Effects of pH, thiol activators, low-molecular weight inhibitors, and proteinase inhibitors (PIs) on general substrate hydrolysis by midgut extracts were determined. Hemoglobinolytic activity was highest in the acidic to mildly acidic pH range, but was maximal at pH 3.5. Addition of thiol-activator...

Journal: :Applied and environmental microbiology 1992
T Coolbear J R Reid G G Pritchard

The cell wall-associated proteinase from Lactococcus lactis subsp. cremoris H2 (isolate number 4409) was released from the cells by treatment with lysozyme, even in the presence of 50 mM calcium chloride. Cell lysis during lysozyme treatment was minimal. The proteinase activity released by lysozyme treatment fractionated on ion-exchange chromatography as three main forms, the molecular masses o...

Journal: :The Biochemical journal 2001
K Oda H Oyama S Ito M Fukiharu Y Miyagawa S Takahashi M Hirose N Kikuchi T Nakayama Y Shibano

Kexstatin I is a potent proteinaceous inhibitor of Kex2 proteinase (EC 3.4.21.61). In the present study we show the molecular cloning, primary structure determination and expression of the gene encoding kexstatin I. We also demonstrate its enhanced activity and specificity for Kex2 proteinase inhibition by rational mutagenesis. The cloned kexstatin I gene encoded a protein of 145 amino acid res...

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