Activation studies of the multiple forms of prochymosin (prorennin)
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چکیده
منابع مشابه
Activation 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...
متن کاملDenaturation 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...
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چکیده ندارد.
15 صفحه اولSynthesis of calf prochymosin (prorennin) in Escherichia coli.
A gene for calf prochymosin (prorennin) has been reconstructed from chemically synthesized oligodeoxyribonucleotides and cloned DNA copies of preprochymosin mRNA. This gene has been inserted into a bacterial expression plasmid containing the Escherichia coli tryptophan promoter and a bacterial ribosome binding site. Induction of transcription from the tryptophan promoter results in prochymosin ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1977
ISSN: 0264-6021
DOI: 10.1042/bj1670429