M. Kouhiyan; B. Shareghi; F. Kouhiyan
Volume 1, Issue 1 , October 2012, , Pages 24-30
Abstract
Pepsin (E.C.3.4.23.1) is a juice gastric aspartic proteinase. It belongs to hydrolyses family. Its monomeris structure is consisting of two lobes that they are similar in size and folding. It consists of a single polypeptide chain of molecular weight 34644 Daltone and 327 aminoacid. Structural analysis ...
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Pepsin (E.C.3.4.23.1) is a juice gastric aspartic proteinase. It belongs to hydrolyses family. Its monomeris structure is consisting of two lobes that they are similar in size and folding. It consists of a single polypeptide chain of molecular weight 34644 Daltone and 327 aminoacid. Structural analysis shows that pepsin contains 1.2% basic residues, 13.1% acidic residues, 46.5% polar residues and 39.2% hydrophobic residues. Structural stability of pepsin was investigated by UV-VIS spectrophotometer and spectrophlorimetry. Spectral measurements were made by sodium phosphate buffer .02M at pH: 2 and temperatures between 30 and 100 º C. It was observed that (1) high considerable enzyme stability, (2) enzyme stability decreases in the presence of urea at pH: 2. (3) thermodynamic parameters decline in the presence of urea. (4) Florescence intensity increase in the presence of urea.
