CHARACTERIZATION AND STRUCTURE OF PINEAPPLE STEM INHIBITOR OF CYSTEINE PROTEINASES

被引：19

作者：

LENARCIC, B

RITONJA, A

TURK, B

DOLENC, I

TURK, V

机构：

[1] Department of Biochemistry, J. Stefan Institute, Ljubljana, Jamova 39

来源：

BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1992年 / 373卷 / 07期

关键词：

CYSTEINE PROTEINASE INHIBITOR; STEM BROMELAIN INHIBITOR; PRIMARY STRUCTURE;

D O I：

10.1515/bchm3.1992.373.2.459

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The complete amino acid sequence of the inhibitor of cysteine proteinases from pineapple stem acetone powder was determined. The inhibitor consists of 52 amino acids and is composed of two polypeptide chains (41 and 11 amino acids) linked via disulphide bonds. It differs from already known sequences in one to four amino acids. Data from its amino acid sequence analysis clearly show that this inhibitor cannot be a member of the cystatin superfamily. The K(i) values for papain, bromelain and cathepsin L were determined.

引用

页码：459 / 464

页数：6

共 13 条

[1] NEW ASSAY FOR CATHEPSIN B1 AND OTHER THIOL PROTEINASES [J].

BARRETT, AJ .

ANALYTICAL BIOCHEMISTRY, 1972, 47 (01) :280-&

[2]

BRZIN J, 1989, INTRACELLULAR PROTEO, P398

[3] VIDEO ENHANCED IMAGING OF THE FLUORESCENT NA+ PROBE SBFI INDICATES THAT COLONIC CRYPTS ABSORB FLUID BY GENERATING A HYPERTONIC INTERSTITIAL FLUID [J].

NAFTALIN, RJ ;

PEDLEY, KC .

FEBS LETTERS, 1990, 260 (02) :187-194

[4] BOVINE CATHEPSIN-S AND CATHEPSIN-L - ISOLATION AND AMINO-ACID-SEQUENCES [J].

DOLENC, I ;

RITONJA, A ;

COLIC, A ;

PODOBNIK, M ;

OGRINC, T ;

TURK, V .

BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1992, 373 (07) :407-412

[5]

GRECO WR, 1979, J BIOL CHEM, V254, P2104

[6]

HENSCHEN A, 1986, ADV METHODS PROTEIN, P244

[7]

LOWRY OH, 1951, J BIOL CHEM, V193, P265

[8]

PERLSTEIN S H, 1973, Journal of Supramolecular Structure, V1, P249, DOI 10.1002/jss.400010309

[9]

RAWLINGS ND, 1990, COMPUT APPL BIOSCI, V6, P118

[10]

REDDY MN, 1975, J BIOL CHEM, V250, P1741

← 1 2 →