บทคัดย่องานวิจัย

หมวดหมู่ : ฐานข้อมูลงานวิจัย

Purification and characterization of a polygalacturonase-inhibiting protein from apple fruit.

Yao, C., Conway, W.S. and Sams, C.E.

Phytopathology. Volume 85, Number 11, Nov 1995. Pages 1373–1377.

1995

บทคัดย่อ

Purification and characterization of a polygalacturonase-inhibiting protein from apple fruit.

A polygalacturonase-inhibiting protein (PGIP) was purified from mature 'Golden Delicious' apple fruit. The protein was cell wall bound and had a molecular mass of 44 to 54 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Chemical deglycosylation of purified apple PGIP released a 34-kDa polypeptide, suggesting that differential glycosylation accounted for the heterogeneity in molecular mass. Apple PGIP showed differential inhibitory activity against five polygalacturonase isozymes purified from Botrytis cinerea grown in liquid culture. However, inhibition was not detected against polygalacturonase extracted from apple fruit inoculated with the same fungus. Kinetic studies suggested a mixed-type inhibition. N-terminal amino acid sequence of apple PGIP shared 96%, 68%, and 60% identity with those from pear, tomato, and bean, respectively.