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Seed proteases and protease inhibitors
Economic Botany, 1970This review, which unavoidably has to be of a highly selective nature, covers the literature through December, 1967, and is concerned with two classes of proteins which are involved in the metabolism of seeds: proteases and protease inhibitors. During germination, proteases degrade protein reserves of seeds with an attendant release of peptides, free ...
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Essays in Biochemistry, 2002
A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases.
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A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases.
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Chemical Reviews, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
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AbstractFor Abstract see ChemInform Abstract in Full Text.
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Proteases and Protease Inhibitors in Neoplasia
1974Although proteases in tumours have been studied for many years [1], their role is far from clear. From a number of comparative studies (summarized in Table 1), however, it can be safely concluded that increased proteolytic activity is often associated with tumours.
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Scandinavian Journal of Clinical and Laboratory Investigation, 1992
The Aspartic proteases (EC 3.4.23) are a group of proteolytic enzymes that share the same catalytic apparatus. Members of the aspartic protease family can be found in different organisms, ranging from humans to plants and retroviruses. The best known sources of aspartic proteases are the stomach of mammals, yeast and fungi, with porcine pepsin as the ...
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The Aspartic proteases (EC 3.4.23) are a group of proteolytic enzymes that share the same catalytic apparatus. Members of the aspartic protease family can be found in different organisms, ranging from humans to plants and retroviruses. The best known sources of aspartic proteases are the stomach of mammals, yeast and fungi, with porcine pepsin as the ...
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Lung Proteases and Protease Inhibitors
1977Homogenates of guinea pig lung show significant protease activity at pH values from 2.2 to 9.9. Perfusion results in increased activity in both acid and alkaline ranges. Protease activity can be extracted by repeated homogenization and sonication of the pellet.
Jeffrey Ihnen, George Kalnitsky
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