Purification and Properties of a Membrane-bound Phospholipase A1 from Mycobacterium phlei
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چکیده
منابع مشابه
Purification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei.
A phospholipase A1 bound tightly to the membranes of Mycobacterium phlei cells was purified approximately 500fold to near homogeneity by extraction with Triton X-100, delipidation with organic solvents, solubilization with sodium dodecyl sulfate, column chromatographies on Sephadex G-200 in the presence of sodium dodecyl sulfate and on DEAE-cellulose in the presence of BRIJ 58, and sodium dodec...
متن کاملPurification and Properties of a Membrane-bound Phospholipase A, from Mycobacterium phlei
A phospholipase A1 bound tightly to the membranes of Mycobacterium phlei cells was purified approximately 500fold to near homogeneity by extraction with Triton X-100, delipidation with organic solvents, solubilization with sodium dodecyl sulfate, column chromatographies on Sephadex G-200 in the presence of sodium dodecyl sulfate and on DEAE-cellulose in the presence of BRIJ 58, and sodium dodec...
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The phospholipid composition of the electron transport particles and coupling factor-depleted electron transport particles of Mycobacterium phlei are the same, but they differ in contents. The accessibility of partially purified phospholipase A to these membrane phospholipids was found to be different. Treatment of membranes of Mycobacterium phlei with phospholipase A impairs the rate of oxidat...
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A simplified method for the preparation of a large amount of crystalline lactate oxygenase from Mycobacterium phlei has been introduced. The crystalline enzyme exhibited one component on polyacrylamide gel electrophoresis and revealed a single homogeneous peak (s~,~ = 12.5 S) in an ultracentrifuge. The enzyme has a typical flavoprotein spectrum, and the prosthetic group was shown to be flak mon...
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The dihydrofolate reductase from Mycobacterium phlei was purified and characterized; it has an Mr of 15 000 and a pI of 4.8. It is competitively inhibited by both methotrexate and trimethoprim, although the affinity is less than for other bacterial dihydrofolate reductases.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)79778-4