The first step in the activation of chicken pepsinogen is similar to that of prochymosin.
نویسندگان
چکیده
Chicken pepsinogen was incubated at pH2.5 with pepstatin. The zymogen activated itself by a sequential mechanism and an intact peptide derived from residues 1-26 in the protein was released in the first step. This peptide was found to inhibit the milk-clotting activities of pig and chicken pepsins and calf chymosin but to different extents.
منابع مشابه
Denaturation studies on natural and recombinant bovine prochymosin (prorennin).
1. Prochymosin in solution in the presence of 8 M-urea is fully unfolded, as indicated by its fluorescence spectrum, fluorescence quenching behaviour and far-u.v.c.d. spectrum. 2. Equilibrium studies on the unfolding of prochymosin and pepsinogen by urea were carried out at pH 7.5 and pH 9.0. The results indicate that the stabilization energies of the two proteins are identical at pH 7.5, but t...
متن کاملActivation studies of the multiple forms of prochymosin (prorennin).
Activation of the four separate components of prochymosin (prorennin) at pH 5.0 demonstrated that each zymogen was the precursor to an electrophoretically distinct chymosin (rennin). When the increase in milk-clotting activity with time was analysed, the mechanism of activation of unfractionated prochymosin, individual prochymosin components, and a mixture of the prochymosin fractions at pH 5.0...
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The effect of mechanical activation on the kinetics of ammoniacal thiosulfate leaching of a refractory oxide gold ore containing 2.8 ppm Au was investigated. The gold extraction of 99.81% was achieved by 16 h leaching of a sample mechanically activated for 60 minutes. The gold extraction observed for a similar reference sample without mechanical activation was only 55%. Studies revealed that le...
متن کاملTransformation of Swine Pepsinogen into Swine Pepsin by Chicken Pepsin
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متن کاملThe activation of bovine pepsinogen. Sequence of the peptides released, identification of a pepsin inhibitor.
Bovine pepsinogen is converted into pepsin by removal of 45 amino acid residues from the NH, terminus of the single polypeptide chain. The complete sequence of the activation peptides has been deduced from two overlapping sets of peptides, one set obtained by autoactivation of the zymogen at pH 2 and the second set from a tryptic digest of maleylated pepsinogen. A peptide derived from the 17 re...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 167 3 شماره
صفحات -
تاریخ انتشار 1977