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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1986-2-12
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pubmed:abstractText |
A new method for purification and crystallization of pig skeletal muscle phosphorylase b is presented. The ease of crystallization in the presence of 1 mM AMP and 1 mM spermine has permitted the study of some physical, chemical and enzymatic properties of the enzyme. The crystalline pig phosphorylase b gave a single band on SDS polyacrylamide gels of the same mobility as rabbit muscle phosphorylase subunit. Ultracentrifugation experiments showed that pig phosphorylase b exists in a dimeric form (S20,w = 8.4 S). No association occurred at 20 degrees C under conditions where rabbit phosphorylase b can be tetramerized; pig phosphorylase b was only 30% associated from dimer to tetramer at 13 degrees C. Pig phosphorylase b is highly stable to freezing and its specific activity did not change appreciably upon prolonged storage in the cold. Pig and rabbit phosphorylases b have comparable Vmax and Km values towards the substrate and the activator. However, there is an essential difference between the two enzymes in that pig phosphorylase b is not significantly inhibited by glucose 6-phosphate, which is a powerful inhibitor of the rabbit enzyme. Two different crystal forms of pig phosphorylase b were obtained which are small for X-ray diffraction studies. Diffusion of spermine into tetragonal crystals of rabbit phosphorylase b resulted in a difference Fourier synthesis at 3 A resolution that showed no strong indication of specific binding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
832
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
248-56
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3935171-Animals,
pubmed-meshheading:3935171-Crystallization,
pubmed-meshheading:3935171-Dithionitrobenzoic Acid,
pubmed-meshheading:3935171-Drug Stability,
pubmed-meshheading:3935171-Kinetics,
pubmed-meshheading:3935171-Molecular Weight,
pubmed-meshheading:3935171-Muscles,
pubmed-meshheading:3935171-Phosphorylase b,
pubmed-meshheading:3935171-Phosphorylases,
pubmed-meshheading:3935171-Protein Binding,
pubmed-meshheading:3935171-Rabbits,
pubmed-meshheading:3935171-Species Specificity,
pubmed-meshheading:3935171-Sulfhydryl Compounds,
pubmed-meshheading:3935171-Swine
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pubmed:year |
1985
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pubmed:articleTitle |
Crystallization of pig skeletal phosphorylase b. Purification, physical and catalytic characterization.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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