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Literature summary for 3.4.21.7 extracted from

  • Huppertz, T.; Uniacke, T.; Kelly, A.L.; Fox, P.F.
    Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum (2006), Int. dairy J., 16, 691-696.
    View publication on PubMed
Search for more literature for 3.4.21.7

Activating Compound

Activating Compound Comment Organism Structure
Blood serum 2.0% equine serum increases plasmin activity by ca.50% when assayed with N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
Blood serum bovine or ovine blood serum do not affect hydrolysis of caseins in milk by plasmin. Equine and particularly porcine serum strongly inhibit casein hydrolysis. Heated serum (70°C for 5 min) from any of the species does not influence plasmin-induced hydrolysis of caseins. Bovine or ovine serum (2%) have no effect on plasmin activity when assayed on N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk. 2.0% porcine serum reduces plasmin activity on this peptide by ca. 40% Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alphas1-casein + H2O
-
 Bos taurus ?
-
 ?
beta-casein + H2O
-
 Bos taurus ?
-
 ?
N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methylcoumarin + H2O
-
 Bos taurus ?
-
 ?