Solubilization and activation of recombinant calf prochymosin from Escherichia coli.
نویسندگان
چکیده
Lah, T., Turk, V. &Pain, R. H. (1984) Biochem. J. 218,601-608 McPhie, P. (1980) J. Biol. Chem. 255,4048-4052 Perlmann, G. E. (1956) Arch. Biochem. Biophys. 65,210-217 Privalov, P. L., Mateo, P. L., Khechinashvili, N. N., Stepanov, V. M. & Revina, L. P. (1981) J. Mol. Biol. 152,445-464 Schlamowitz, M., Peterson, L. V. & Wissler, F. C. (1961) Arch. Biochem. Biophys. 92,58-68 Shewale, J. G. & Tang, J. (1984) Proc. Natl. Acad. Sci. U.S.A. 81,
منابع مشابه
Bacterial Expression and Functional Characterization of A Naturally Occurring Exon6-less Preprochymosin cDNA
Chymosin (Rennin EC 3.4.23.4), an aspartyl proteinase, is the major proteolytic enzyme in the fourthstomach of the unweaned calf, and it is formed by proteolytic activation of its zymogene, prochymosin.Following the cloning of synthesized cDNAs on mRNA pools extracted from the mucosa of the calf fourthstomach, we have identified an alternatively spliced form of preprochymosin ...
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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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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 13 6 شماره
صفحات -
تاریخ انتشار 1985