Literature DB >> 5144

Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species.

G J Ronda, W Gaastra, J J Beintema.   

Abstract

The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates.

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Year:  1976        PMID: 5144     DOI: 10.1016/0005-2744(76)90331-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  The molecular evolution of pancreatic ribonuclease.

Authors:  J J Beintema; W Gaastra; J A Lenstra; G W Welling; W M Fitch
Journal:  J Mol Evol       Date:  1977-09-20       Impact factor: 2.395

2.  Structural investigation of catalytically modified F120L and F120Y semisynthetic ribonucleases.

Authors:  V S deMel; M S Doscher; M A Glinn; P D Martin; M L Ram; B F Edwards
Journal:  Protein Sci       Date:  1994-01       Impact factor: 6.725

3.  Primary structure of pronghorn pancreatic ribonuclease: close relationship between giraffe and pronghorn.

Authors:  J J Beintema; W Gaastra; J Munniksma
Journal:  J Mol Evol       Date:  1979-11       Impact factor: 2.395

  3 in total

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