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The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae.
The enzyme, protoporphyrinogen oxidase, associated with purified mitochondria isolated from Saccharomyces cerevisiae was solubilized by sonic treatment in the presence of detergent and partially purified and was insensitive to cyanide, 2,4-dinitrophenol, and azide whereas it was inhibited in the absence of Cu-2- or Co-2+ ions, high ionic strength, heme, or hemin. Expand
Studies in disorders of muscle. IX. Glycogen storage disease primarily affecting skeletal muscle and clinically resembling amyotonia congenita.
Three infants (siblings) with flaccid weakness of skeletal muscle are described with postmortem findings in two and the anatomic disorder in these infants consisted of excess glycogen storage producing its main effect in striated muscle. Expand
Lipoquinones of Escherichia coli.
Aerobic and anaerobic coproporphyrinogenase activities in extracts from Saccharomyces cerevisiae.
Coproporphyrinogenase was isolated from mitochondrial extracts of Saccharomyces cerevisiae following mechanical disruption and purified 150-fold by a procedure involving ion exchange chromatography and gel filtration and catalyzed the conversion of coproporpharinogen III to protoporphyr inogen IX under both aerobic and anaerobic conditions. Expand
Polysaccharides associated with wood cellulose.
- W. Polglase
- Chemistry, Medicine
- Advances in carbohydrate chemistry
This chapter discusses the polysaccharides associated with wood cellulose, and it is anticipated that a combination of these methods will eventually provide important data on the molecular weight and distribution of the associated polysarcharides, as well as on the nature of the associative forces. Expand
The specificity of leucine aminopeptidase. III. Action on diastereoisomers.
Degradative studies on streptomycin.
The van der Waals factor in carboxypeptidase interaction with inhibitors and substrates.
Studies on human glycogen. II. Sedimentation in the ultracentrifuge.
- W. Polglase, D. Brown, E. L. Smith
- Biology, Medicine
- The Journal of biological chemistry
- 1 November 1952
It was found that glycogen from a patient (N. D.) with a glycogen storage disorder of muscle’ differed from normal samples in the distribution of scdimenting components, which is not continuous in liver glycogen preparations. Expand
The specificity of leucine aminopeptidase; optical and side chain specificity.