YAKHAK HOEJI (약학회지)
- Volume 33 Issue 6
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- Pages.339-344
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- 1989
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- 0377-9556(pISSN)
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- 2383-9457(eISSN)
Studies on Higher Fungi in Korea (V) -N-Terminal Amino Acid Sequence and Some Properties of Proteolytic Enzyme from Sarcodon aspratus-
한국산 고등균류에 관한 연구(제 5보) -능이 중 단백분해효소의 특성과 N-말단 아미노산배열-
- Eun, Jae-Soon (Jeonju Woosuk University) ;
- Yang, Jae-Hean (Jeonju Woosuk University) ;
- Lee, Tae-Kyu (Jeonju Woosuk University) ;
- Choi, Dong-Seong (Jeonju Woosuk University)
- Published : 1989.12.28
Abstract
The alkaline protease produced by Sarcodon aspratus(Berk) S. Ito. was purified from its fruit bodies. The enzyme was purified by using ammonium sulfate fractionation, tris-acryl CM-cellulose column chromtography and chromatofocusing. The protease migrated as one major band with a molecular weight of about 29,000 dalton on sodium dodecylsulfate-polyacrylamide gel electrophoresis. The amino acid sequence of the N-terminal residues(21) of the enzyme was determined by automated sequence analysis. The sequence was Val-Thr-Thr-Lys-Gln-Thr-Asn-Ala-Pro-Trp-Gly-Leu-Gly-Asn-Ile-Ser-Thr-Thr-Asn-Lys-Leu. Comparison of this sequence with the N-terminal sequence of the p-roteinase K from Tritirachium album showed high similarity, i. e. 57.8% identical residues. The protease displayed a relatively high stability in sodium dodecyl sulfate.