Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch
| Autor: | Inna P. Gladysheva, S.D. Varfolomeyev, Nadezhda V. Sorokina, Nathalia I. Larionova, Stepan S. Vartanov |
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| Rok vydání: | 1997 |
| Předmět: |
Plasma Substitutes
Bioengineering Polysaccharide Applied Microbiology and Biotechnology Biochemistry Hydroxyethyl Starch Derivatives Sepsis medicine Chymotrypsin Humans Molecular Biology Plant Proteins chemistry.chemical_classification biology Kunitz STI protease inhibitor Chemical modification Shock General Medicine Trypsin Enzyme chemistry Enzyme inhibitor biology.protein Leukocyte Elastase Half-Life Biotechnology medicine.drug Conjugate |
| Zdroj: | Applied Biochemistry and Biotechnology. 62:175-182 |
| ISSN: | 1559-0291 0273-2289 |
| DOI: | 10.1007/bf02787993 |
| Popis: | The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, Ki, of bovine trypsin, alpha-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation. |
| Databáze: | OpenAIRE |
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