We have located links that may give you full text access.
Purification and Properties of Intracellular Proteinase from Streptococcus cremoris.
Applied Microbiology 1975 November
Proteolytic activity in the extract from the cells of Streptococcus cremoris increased in the presence of casein, lactose, glucose, and CaCl(2) in the media but was negligibly detectable in the extract of the cells harvested from the culture containing succinate or citrate. The intracellular proteinase from S. cremoris harvested from tomato medium was purified 150-fold in this experiment. The enzyme had a molecular weight of 140,000, optimum pH at 6.5 to 7.0, and maximum activity at 30 C. The proteinase was activated by Ca and inhibited by Zn, Cu, Hg, Fe, ethylenediaminetetraacetate, and sodium lauryl sulfate. The K(m) value of the enzyme towards each casein fraction was almost the same, and the V(max) of the enzyme towards alpha(s)-casein was smaller than those towards the other casein fractions.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app