Literature DB >> 477907

The use of dipeptide-p-nitranilides for the study of aminopeptidase specificity.

M Rybák, E Kasafírek, B Rybáková, E Simonianová.   

Abstract

The use of dipeptide-p-nitranilides for the study of 2 placental aminopeptidases separated on Sephadex G200 helped in establishing some regular features of their specifities. The high-molecular (320,000 daltons) one prefers Phe in position P'1 to Leu, whereas the lower-molecular aminopeptidase (145,000 daltons) prefers Leu. The high-molecular aminopeptidase splits very slowly the N-terminal Leu when Gly is in adjacent position. Leu-Gly-p-NA is therefore an inhibitor of this AP.

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Year:  1979        PMID: 477907     DOI: 10.1007/bf01949902

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  3 in total

1.  [Method for quantitative evaluation of the biological effects of kinins on isolated uterus of rats].

Authors:  M Rybák
Journal:  Cesk Fysiol       Date:  1971

2.  On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain.

Authors:  I Schechter; A Berger
Journal:  Biochem Biophys Res Commun       Date:  1968-09-06       Impact factor: 3.575

3.  The hydrolysis of some L-amino acid-p-nitranilides with the normal and pregnant's serum aminopeptidases.

Authors:  M Rybák; B Rybáková; M Petáková
Journal:  Experientia       Date:  1978-01-15
  3 in total

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