Author
W.E. Pricer
Other affiliations: Albert Einstein College of Medicine
Bio: W.E. Pricer is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Sialic acid & Asialoglycoproteins. The author has an hindex of 12, co-authored 13 publications receiving 2773 citations. Previous affiliations of W.E. Pricer include Albert Einstein College of Medicine.
Papers
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567 citations
TL;DR: The purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associated with the membranes is described, which indicates a high degree of aggregation in the final, water-soluble preparation.
555 citations
TL;DR: In order to provide some definitive information on the mechanism of conversion ofadenosine to adenosine-5’-phosphate, an enzyme preparation has been obtained which catalyzes the reaction.
433 citations
359 citations
TL;DR: Evidence is presented to identify plasma membranes of liver as the major locus of binding for circulating glycoproteins and the binding process involves a dual role for sialic acid in that its presence on the membranes is essential, whereas its existence on the glycoprotein is incompatible with binding.
356 citations
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TL;DR: A rapid method based on a defined methanol-chloroform-water mixture for the quantitative precipitation of soluble as well as hydrophobic proteins from dilute solutions (e.g., column chromatography effluents) has been developed.
3,842 citations
TL;DR: This is a record of the concentrations of the nonenzyme components of the Embden-Meyerhof system in mouse brain measured at brief intervals after the production of complete ischemia by decapitation, which resulted in increases in glycolytic rates of at least 4to 7-fold in different experimental groups of mice.
2,179 citations
TL;DR: The ratio of P32 to Cl4 in the product was closely similar to that of the labeled P-choline, suggesting incorporation of both phosphorus and choline as an intact unit into a phospholipide, presumably lecithin.
1,614 citations
TL;DR: This chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity.
Abstract: Publisher Summary Lectins play an important role in the development of immunology. Lectins also find application in serological laboratories for typing blood and determining secretor status, separating leucocytes from erythrocytes, and agglutinating cells from blood in the preparation of plasma. They serve as reagents for the detection, isolation, and characterization of carbohydrate-containing macromolecules, including blood-group antigens. In their interaction with saccharides, lectins serve as models for carbohydrate-specific antibodies, with the important advantage to purify lectins in gram quantities. Lectins are classified according to their carbohydrate-binding specificity that includes D-mannose(D-glucose)-binding lectins and 2-acetamido-2-deoxy-D-glucose-binding lectins. The chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity. The chapter also describes the cell-binding and biological properties of lectins. The chapter concludes with the description of several glycopeptide structures showing the carbohydrate-binding loci with which various lectins interact.
1,540 citations
TL;DR: The only firmly established function of carnitine is its function as a carrier of activated fatty acids and activated acetate across the inner mitochondrial membrane, and the regulation of its synthesis is still incompletely understood.
Abstract: Carnitine was detected at the beginning of this century, but it was nearly forgotten among biochemists until its importance in fatty acid metabolism was established 50 years later. In the last 30 years, interest in the metabolism and functions of carnitine has steadily increased. Carnitine is synthesized in most eucaryotic organisms, although a few insects (and most likely some newborn animals) require it as a nutritional factor (vitamin BT). Carnitine biosynthesis is initiated by methylation of lysine. The trimethyllysine formed is subsequently converted to butyrobetaine in all tissues; the butyrobetaine is finally hydroxylated to carnitine in the liver and, in some animals, in the kidneys (see Fig. 1). It is released from these tissues and is then actively taken up by all other tissues. The turnover of carnitine in the body is slow, and the regulation of its synthesis is still incompletely understood. Microorganisms (e.g., in the intestine) can metabolize carnitine to trimethylamine, dehydrocarnitine (b...
1,530 citations