Purification and characterization of the inactive Ca2+, Mg2+-activated adenosine triphosphatase of the unc A- mutant Escherichia coli AN120. |
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Authors: | P D Bragg C Hou |
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Institution: | Universität Konstanz, Fachbereich Biologie, D — 775 Konstanz West Germany |
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Abstract: | Resealing of erythrocyte ghosts in the presence of 4.5 mm Ca2+ induces the segregation of small membrane vesicles with a very high phospholipid:protein ratio and a high lysolecithin content. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate indicates that the vesicles consist mainly of the high molecular spectrin peptides, the Ca2+-induced increase of band IIa (Mr 198,000) which is not extractable at low ionic strength, and a weak peptide band in the 72,000 Mr region. Ca2+ ghosts and vesicles show significant differences with regard to the specific activities of several membrane-associated enzymes. The segregated vesicles dispose of an efficient outwarddirected Ca2+-transport system. |
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