Subcloning and Expression of Prochymosin cDNA
نویسندگان
چکیده
منابع مشابه
Prochymosin expression in Bacillus subtilis.
Prochymosin (PC) sequence was cloned in Bacillus subtilis using two kinds of plasmid constructions. In plasmid pSM316 the cDNA was inserted to obtain the intracellular expression of the enzyme. The enzyme turned out to be expressed in an insoluble form which could be converted to native enzyme under proper denaturing and refolding conditions. The levels of intracellular expression of PC were fu...
متن کاملHeterologous Expression of Bovine Prochymosin in Pichia pastoris GS115
Objectives: In present research we evaluate the expression of this critical enzyme in a eukaryotic system for future use in cheese industry. Materials and Methods: We have cloned bovine prochymosin gene in methylotrophic yeast, P. pastoris, using pPIC9K as an expression vector. The recombinant plasmid was transformed into the host by electroporation, and it was expre...
متن کاملCodon optimization and cloning of bovine prochymosin gene for proper expression in tobacco plant
Bovine chymosin enzyme is one of the most commonly used enzymes in the dairy industry. The production of this enzyme from its natural source does not meet the needs of this huge industry. The production of recombinant bovine chymosin in plants can be a good alternative to native enzyme. Insertion and expression of foreign genes in plants can occur in the nucleus and chloroplast organelles. The ...
متن کاملBacterial 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 ...
متن کاملMasking of signal sequences in CREC proteins by cDNA subcloning in epitope vectors.
Tsukumo and colleagues (1) have recently reported that a proline residue at position 2 from the signal peptide cleavage site determines the export of nucleobindin 1 from the endoplasmic reticulum (ER) and subsequent transport to the Golgi. They also studied the localization of three CREC proteins, reticulocalbin, calumenin, and Cab45 that contain a proline at position 2 from the N-terminal sign...
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ژورنال
عنوان ژورنال: Biotechnology & Bioindustry
سال: 1986
ISSN: 0205-2067
DOI: 10.1080/02052067.1986.10824260