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Author Chi, CHENG-WU ♦ Liu, HUA-ZHEU ♦ Liu, CHI-YIN ♦ Chibber, Bakshy A. K. ♦ Castellino, Francis J.
Source J-STAGE
Content type Text
Publisher JAPAN ANTIBIOTICS RESEARCH ASSOCIATION
Language English
Abstract A group of leupeptin analogues was found in Streptomyces griseus strain 254, isolated from a soil sample from Fujian Province, China. The inhibitors excreted in the culture filtrate were purified by adsorption on macroporous resin, followed by sequential ion exchange chromatography on DEAE-52 cellulose, CM-32 cellulose and affinity chromatography with immobilized trypsin. The preparation thus obtained was further purified by preparative HPLC. Several major components were found and characterized, which possessed different inhibitory properties toward trypsin. Based upon amino acid and mass spectrophotometric analysis, these peptides were placed in four major structural categories, viz., R-Val-Val-argininal, R-Leu-Leu-argininal, R-Ile-Ile-argininal and R-Thr-Thr-argininal, this latter component representing a newly identified leupeptin analogue. The structural variability of the R-group was partly responsible for the multiplicity of the peaks obtained with HPLC. All peptides displayed varying degrees of inhibitory activity toward proteases involved in blood coagulation and fibrinolysis, including plasmin, factor Xa, activated protein C and thrombin. Among these peptide inhibitors, the molecule containing threonine showed the strongest inhibitory activity.
ISSN 00218820
Learning Resource Type Article
Publisher Date 1989-10-25
e-ISSN 18811469
Journal The Journal of Antibiotics(antibiotics1968)
Volume Number 42
Issue Number 10
Page Count 7
Starting Page 1506
Ending Page 1512


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