Degradation of Band‐3 Glycoprotein in vitro by a Protease Isolated from Human Erythrocyte Membranes
1982
GOLOVTCHENKO‐MATSUMOTO, Anne Marianne | MATSUMOTO, Isamu | Osawa, T (Toshiaki)
The use of soybean‐trypsin‐inhibitor‐Sepharose‐4B to purify a protease present in human erythrocyte membranes is described. The fraction bound in the presence of calcium to the affinity adsorbent is active on band‐3 glycoprotein in a non‐ionic detergent solulion at neutral pH. Band‐3 glycoprotein is degraded into components having the mobilities of the proteins of bands 4.5, 7 and of lower molecular weights. When calcium is omittcd from the membrane extract, an inactive form of this enzyme can be purified. By DEAE‐cellulose chromatography this inactive form can be convcrted into the active form, presumably by dissociation of an enzymeinhibitor complex.
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