Inhibition of alpha 2-macroglobulin-bound trypsin by soybean trypsin inhibitor.
نویسندگان
چکیده
منابع مشابه
A Soybean Trypsin Inhibitor
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 ...
متن کاملCrystalline Soybean Trypsin Inhibitor
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 کاملIsolation 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 کاملThe Action of Crystalline Trypsin and Soybean Trypsin Inhibitor on the Clotting of Blood by Staphylocoagulase *
The mechanism of the coagulation of blood by staphylocoagulase and the relation of this process to physiological clotting present many unsolved problems. Evidence has been advanced for the concept that coagulase reacts with a plasma component (coagulase reacting factor CRF) which is distinct from prothrombin.5'4'1S1 The formation of an intermediate complex has been inferred from the shortening ...
متن کاملInhibition of proteases by alpha 2-macroglobulin. The role of lysyl amino groups of trypsin in covalent complex formation.
The lysyl amino groups of bovine trypsin were covalently modified by acetylation, succinylation, or reductive methylation. The enzymatically active derivatives were still capable of reaction with alpha 2-macroglobulin (alpha 2M), although to a lesser extent than native enzyme. The resulting enzyme-alpha 2M complexes, however, were much more susceptible to dissociation by sodium dodecyl sulfate ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)43372-8