Results 141 to 148 of about 12,284 (148)
To understand the mechanism of the maturation of various proteins in protein‐storage vacuoles, we purified a 48‐kDa aspartic endopeptidase composed of 32‐kDa and 16‐kDa subunits from castor bean. Immunocytochemical and cell fractionation analyses of the endosperm of maturing castor bean seed showed that the aspartic endopeptidase was localized in the ...
N, Hiraiwa +3 more
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AbstractThe unit describes a basic protocols utilized to obtain milligram amounts of enzymatically active, pure recombinantPlasmodiumplasmepsins and "short" human pseudocathepsin D. Specific details for the expression and purification ofPlasmodium falciparumplasmepsin 2 and "short" human pseudocathepsin D in zymogen form are described in this chapter ...
Bret B, Beyer +2 more
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Protein hydrolysis under acidic conditions can improve the product quality, nutrient availability, and cost efficiency, particularly when neutral or alkaline enzymes are ineffective. Six fungal aspartic endopeptidases (FAPs) were recombinantly expressed as active enzymes in Komagataella phaffi, with peak activity between 30-50 °C and pH 3.0-4.0 ...
Uzair Ahmed +7 more
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Recruitment of Lysosomal Cysteine and Aspartic Endopeptidases as Digestive Enzymes
Walter R. Terra +2 more
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Plant Breeding, 1991
AbstractWheat, rye and wheat‐rye addition lines have been investigated regarding their developmental and organ‐specific isozyme patterns of aspartate amino‐transferase (AAT) and endopeptidase (EP). Evidence is given, that development‐specific isozymes of AAT are encoded by chromosomes 3R and 4R of ‘Imperial’ rye which can be used as biochemical markers
Sonja Drefahl, R. Buschbeck
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AbstractWheat, rye and wheat‐rye addition lines have been investigated regarding their developmental and organ‐specific isozyme patterns of aspartate amino‐transferase (AAT) and endopeptidase (EP). Evidence is given, that development‐specific isozymes of AAT are encoded by chromosomes 3R and 4R of ‘Imperial’ rye which can be used as biochemical markers
Sonja Drefahl, R. Buschbeck
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Crystal structure analysis of the D-aspartic acid specific endopeptidase, paenidase, from prokaryote
Satoru Nirasawa
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