Soybean Trypsin Inhibitors Inhibit Trypsin-like and Basic Proteinase Activities of Cultured-Fishes
نویسندگان
چکیده
منابع مشابه
Isolation and Characterization of Trypsin Inhibitors (Kunitz Soybean Trypsin Inhibitor, Bowman-birk Inhibitor) in Soybean
Soybean (Glycine max (L.) Merr.) has emerged as one of the most economical and nutritious foods. Kunitz Soybean Trypsin Inhibitor (KSTI) and Bowman -Birk Inhibitor (BBI) are the two major trypsin inhibitors in soybeans. The ingested soybean trypsin inhibitors cause growth depression as demonstrated in different animal species and human. The main part of the present study was devoted to isolatio...
متن کاملPolyacrylamide-gel electrophoresis of soybean whey proteins and trypsin inhibitors.
Polyacrylamide·.g~1 electrophoresis with glycine buffer (pH 9.2) containing 8 M urca separated soybean whey proteins into at least 24 bands. In contrast, ultracentrifugation indicated only 2 fractions; moving-boundary electrophoresis, 8-9 components; and column chromatography, 13 or more proteins. A prominent, fast-moving band in the gel pattern appeared to be identical to crystalline soybean t...
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Five trypsin and cu-chymotrypsin inhibitors which have low molecular weights (ranging from 6800 to 8600) and are present in soybean seeds of the Tracy variety have been isolated and purified, and single crystals which give x-ray diffraction data beyond 3-A spacings have been obtained from one of them. The trypsin inhibitor crystallizes in a monoclinic unit cell of symmetry P2, and dimensions a ...
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A study has been made of the general properties of crystalline soybean trypsin inhibitor. The soy inhibitor is a stable protein of the globulin type of a molecular weight of about 24,000. Its isoelectric point is at pH 4.5. It inhibits the proteolytic action approximately of an equal weight of crystalline trypsin by combining with trypsin to form a stable compound. Chymotrypsin is only slightly...
متن کاملA fluorometric determination of trypsin-like amidase activity and activity of trypsin inhibitors in serum.
The activity of crystalline trypsin and the trypsin-like amidase activity and the activity of trypsin inhibitors in serum were measured fluorometically, with a-benzoyl--L-arginine--na phthylamide (BANA) as substrate. The method is simpler and more sensitive than the colorimetric method based on the Bratton-Marshall reaction. Serum of pancreatectomized dogs hydrolyzed BANA at a significant rate,...
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ژورنال
عنوان ژورنال: Fisheries science
سال: 1998
ISSN: 0919-9268
DOI: 10.2331/fishsci.64.935