Chemical Modification of Amino Groups inMucor mieheiAspartyl Proteinase, Porcine Pepsin, and Chymosin. II. Conformational Stability
نویسندگان
چکیده
منابع مشابه
Chemical modification of carboxyl groups in porcine pepsin.
Carboxyl groups i n porcine pepsin were chemically modified "by the carbodiimide reaction using waterrsoluble l-ethyl-3-(3-dimethylaminopropyl) carbodiimide and amino acid esters as nucleophiles. The modification resulted in profound changes in the a c t i v i t i e s , specificity and.some physicochemical properties of the enzyme. These include* (1) significant decrease in milk clotting activi...
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As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the s...
متن کاملRelease and recovery of porcine pepsin and bovine chymosin from reverse micelles: a new technique based on isopropyl alcohol addition.
After complete solubilization by the direct method, porcine pepsin was not released from AOT in isooctane reverse micelles even under aqueous-phase conditions which would not ordinarily allow uptake. Similarly, bovine chymosin, once forward-transferred at a pH below its isoelectric point, was not back-transferred into an aqueous contact phase buffered at a pH value above its isoelectric point. ...
متن کاملEffect of N-linked glycosylation on the aspartic proteinase porcine pepsin expressed from Pichia pastoris.
A study was undertaken to examine the effects of N-linked glycosylation on the structure-function of porcine pepsin. The N-linked motif was incorporated into four sites (two on the N-terminal domain and two on the C-terminal domain), and the recombinant protein expressed using Pichia pastoris. All four N-linked recombinants exhibited similar secondary and tertiary structure to nonglycosylated p...
متن کاملModulating the conformational stability of triple-helical collagen by chemical modification
Collagen is composed of a triple helix of peptides with the sequence (XaaYaaGlY)n, where Xaa is often L-proline (Pro) and Yaa is often 4(R)-hydroxy-L-proline (Hyp). Each strand of collagen adopts a polyproline-II-Iike conformation. Natural collagen is found in approximately 19 different types, and is the most prevalent protein in animals. Triple helices comprised of the peptide (ProHypGly)lO ha...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1991
ISSN: 0002-1369
DOI: 10.1080/00021369.1991.10870916