검색 상세

PURIFICATION, CHARACTERIZATION OF AN ANTIFUNGAL PROTEINS FROM PHARBITIS NIL SEED

Lee, So-Young (College of Pharmacy, Pusan National University) , Jang, Kyung-Suk (College of Pharmacy, Pusan National University) , Lee, Bok-Luel (College of Pharmacy, Pusan National University)

Plant molecular biology and biotechnology research center Annual report, 1994, 1994, 231-240

원문보기

초록/요약moremore
We have isolated and purified to homogeneity two antifungal proteins (named P1 and P2) from Pharbitis nil seeds by measuring the inhibition zone of Botritis cinerea growth. They have a molecular weight 6kDa on SDS-polyacrylamide gel. Partial amino acid sequence analysis on trypsin treated fragments show sequence similarity with that of chitin binding domains, which were shown in bean chitinase, hevein and tobacco chitinase. Purified antifungal proteins exhibit antifungal activities for B. cinerea, Phytophthorea capsici and Fusarium oxysporum. Their N-terminal amino acid was blocked. We have determined their partial amino acid sequences, which have been obtained fragments by trypsin for reduced and alkylated P1 and P2.
We have isolated and purified to homogeneity two antifungal proteins (named P1 and P2) from Pharbitis nil seeds by measuring the inhibition zone of Botritis cinerea growth. They have a molecular weight 6kDa on SDS-polyacrylamide gel. Partial amino acid sequence analysis on trypsin treated fragments show sequence similarity with that of chitin binding domains, which were shown in bean chitinase, hevein and tobacco chitinase. Purified antifungal proteins exhibit antifungal activities for B. cinerea, Phytophthorea capsici and Fusarium oxysporum. Their N-terminal amino acid was blocked. We have determined their partial amino acid sequences, which have been obtained fragments by trypsin for reduced and alkylated P1 and P2.
목차moremore
Ⅰ. Abstract = 231
Ⅱ. Introduction = 231
Ⅲ. Material and Methods = 232
...
Ⅰ. Abstract = 231
Ⅱ. Introduction = 231
Ⅲ. Material and Methods = 232
Ⅳ. Results and Discussion = 234