Literature DB >> 5677534

Hydrolysis at arginylproline in polypeptides by clostridiopeptidase B.

W M Mitchell.   

Abstract

Clostridiopeptidase B, a sulfhydryl protease from Clostridium histolyticum, hydrolyzes the arginylproline bond in the synthetic polypeptide methionyllysyl-bradykinin. Hydrolysis also occurs at a reduced rate at the lysylarginine bond, further delineating the environment necessary for the minor proteolysis seen with this enzyme at lysine residues. The specificity of clostridiopeptidase B differs from trypsin, which hydrolyzes this synthetic polypeptide only at the lysylarginine bond.

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Year:  1968        PMID: 5677534     DOI: 10.1126/science.162.3851.374

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  4 in total

1.  Improved enzymatic isolation of fibroblasts for the creation of autologous skin substitutes.

Authors:  Hongjun Wang; Clemens A Van Blitterswijk; Marion Bertrand-De Haas; Arnold H Schuurman; Evert N Lamme
Journal:  In Vitro Cell Dev Biol Anim       Date:  2004 Sep-Oct       Impact factor: 2.416

2.  Reverse action of hydrolases in frozen aqueous solutions.

Authors:  M Hänsler; H D Jakubke
Journal:  Amino Acids       Date:  1996-09       Impact factor: 3.520

3.  Amino acid sequence of the acidic Kunitz-type trypsin inhibitor from winged-bean seed [Psophocarpus tetragonolobus (L.) DC].

Authors:  J B Caldwell; P M Strike; A A Kortt
Journal:  J Protein Chem       Date:  1990-08

4.  Clostripain, the Missing Link in the Enzyme Blend for Efficient Human Islet Isolation.

Authors:  Magnus Ståhle; Aksel Foss; Bengt Gustafsson; Marko Lempinen; Torbjörn Lundgren; Ehab Rafael; Gunnar Tufveson; Olle Korsgren; Andrew Friberg
Journal:  Transplant Direct       Date:  2015-06-24
  4 in total

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