Literature DB >> 4563931

Studies on the specificity of chymosin (rennin). I. Kinetic parameters of the hydrolysis of synthetic oligopeptide substrates.

M N Raymond, J Garnier, E Bricas.   

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Year:  1972        PMID： 4563931     DOI： 10.1016/s0300-9084(72)80098-1

Source DB:  PubMed          Journal:  Biochimie        ISSN： 0300-9084            Impact factor:   4.079


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  5 in total

1.  Structural aspects of the milk clotting process. Comparative features with the blood clotting process.

Authors:  P Jollès
Journal:  Mol Cell Biochem       Date:  1975-05-30       Impact factor: 3.396

2.  Peptide substrates for chymosin (rennin). Interaction sites in kappa-casein-related sequences located outside the (103-108)-hexapeptide region that fits into the enzyme's active-site cleft.

Authors:  S Visser; C J Slangen; P J van Rooijen
Journal:  Biochem J       Date:  1987-06-15       Impact factor: 3.857

3.  The purification and properties of a single chicken pepsinogen fraction and the pepsin derived from it.

Authors:  M L Green; J M Llewellin
Journal:  Biochem J       Date:  1973-05       Impact factor: 3.857

4.  Calf chymosin as a catalyst of peptide synthesis.

Authors:  C A Abdel Malak
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

5.  Characterization of the amino acids of bovine fibrinogen involved in the fibrinogen-thrombin interaction of the blood clotting process. Comparison with the milk clotting process.

Authors:  N M Kaye; P Jollès
Journal:  Mol Cell Biochem       Date:  1978-08-16       Impact factor: 3.396
  5 in total

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