A Nonproteolytic “Trypsin-like” Enzyme
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چکیده
منابع مشابه
Thrombokinase of the Blood as Trypsin-Like Enzyme
Thrombokinase of the blood, while resembling enterokinase in its role of activator, is more closely analogous to trypsin in its intrinsic origin. It probably arises from a plasma precursor; but it is different from plasmin (fibrinolysin). Like trypsin, thrombokinase can activate prothrombin without the aid of other factors; however, it is potentiated by platelets plus calcium. Unlike certain ti...
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The existence of a trypsin-like enzyme (TLE) in acrosomes ofepididymal spermatozoa was confirmed and was further demonstrated to be present in acrosomes of ejaculated and capacitated spermatozoa. TLE rapidly removes the zona pellucida of the ovum. Extracts of acrosomes of ejaculated spermatozoa contain an inhibitor that is separated from the TLE by purification of the TLE. The inhibitor of TLE ...
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Exogenous proteolytic enzyme supplementation is required in certain disease conditions in humans and animals and due to compelling reasons on use of more plant protein ingredients and profitability in animal feed industry. However, limitations on their utility in diet are imposed by their pH specificity, thermolabile nature, inhibition due to a variety of factors and the possibility of intestin...
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dehydrogenase (Rose et al., 1969). The ,H labelling of ['HI lactate in 2H,0 and the 'H labelling of [2H]lactate in 'H,O has been studied. A comparison of the exchange in whole cells and lysates has also been undertaken. The detailed measurement of exchange kinetics permitted by the n.m.r. technique has revealed the dependence of the exchange on the different enzyme activities and on the triose ...
متن کاملThe export of a trypsin inhibitor from Ehrlich ascites cells that does not inhibit a trypsin-like enzyme on the surface of these cells.
Vertebrate skeletal myosin is hexameric, comprising two heavy chains and four light chains. A regulatory, ‘phosphorylatable’ light chain is thought to reside at each of the two hinge regions between the myosin heads and the tail of the molecule, whereas each of the two heads contains one ‘alkali’ light chain, of which there are two species. These heads, or subfragment-1 (Sl) regions, are readil...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1971
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.48.3.278