منابع مشابه
Purification and characterization of chicken pepsinogen and chicken pepsin.
Chicken pepsinogen was extracted from the forestomach of chicken and purified by the consecutive application of acetone precipitation, chromatography on diethylaminoethyl cellulose, and gel filtration on Sephadex G-100. The purified pepsinogen was homogeneous on disc electrophoresis and sedimented as monodisperse material. Chicken pepsin was obtained by the activation of the pure zymogen at pH ...
متن کاملTransformation of Swine Pepsinogen into Swine Pepsin by Chicken Pepsin
Activation of swine pepsinogen with chicken pepsin results in the formation of swine pepsin. Activation of chicken pepsinogen with swine pepsin results in the formation of chicken pepsin. The structure responsible for the species specificity of the enzyme is therefore present in the inactive precursor.
متن کاملPrimary structure of human pepsinogen gene.
A recombinant clone, which covers the pepsinogen gene in a single insert, has been isolated by screening a library of human genomic DNA, using a swine pepsinogen cDNA as a probe. Sequence analysis of coding DNA segments of the clone revealed that the pepsinogen gene occupies approximately 9.4-kilobase pairs of the genomic DNA and is separated into nine exons by eight introns of various lengths....
متن کاملChicken and rabbit antibodies against porcine pepsinogen A.
Isolated porcine pepsinogen A was used for the preparation of polyclonal rabbit and polyclonal chicken anti-pepsinogen A antibodies. Immunochemical properties of both immunoglobulin fractions were compared. The rabbit anti-serum was further purified using immobilized porcine pepsinogen A on magnetic cellulose beads and the resulting anti-pepsinogen A fraction proved to be applicable for the sep...
متن کاملThe first step in the activation of chicken pepsinogen is similar to that of prochymosin.
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.
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1983
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1983.tb07710.x