Calf chymosin as a catalyst of peptide synthesis
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چکیده
منابع مشابه
Calf chymosin as a catalyst of peptide synthesis.
Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a c...
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چکیده ندارد.
The primary structure of calf chymosin.
The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residu...
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The aminolysis of a mildly activated aminoacid ester, benzyloxycarbonyl-L-phenylalanine cyanomethyl ester, by glycine esters in the presence of catechol has been studied as a model of catalysis by RNA cis-vicinal-diol systems in protein biosynthesis. Catechol accelerated the aminolysis, especially in the presence of bases, probably by nucleophilic catalysis.
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An efficient, simple and convenient route is described for the synthesis of biscoumarin (3,3'-(arylmethylene) bis (4-hydroxy-2H-chromen-2-one)) by using of recyclable catalyst TiO2@KSF. In this Method, we synthesis biscoumarin derivatives via 3multi-component reactions (3MCRs) of two equivalent 4-hydroxycoumarin with one equivalent of aromatic aldehydes using 20 mg nano TiO2@KSF as homogeneous ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1992
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2880941