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W C PARKER

Publications and source records attributed to W C PARKER.

14 recordsLinked to original sources
PubMed1963

ADDITIONAL STUDIES ON THE TRANSFERRINS OF CORD SERUM AND CEREBROSPINAL FLUID; VARIATION IN CARBOHYDRATE PROSTHETIC GROUPS.

Serum transferrins have been examined in 392 samples from full-term infants and from premature infants at various stages of growth. The characteristic transferrin pattern of the infants by starch gel electrophoresis contained a single prominent iron-binding component accompanied by 4 faint, slower migrating components. An additional faint component was present in the sera of infants heterozygous for a transferrin variant. The faint components migrated slightly more rapidly than the corresponding components in the stepwise pattern produced by the action of neuraminidase in removing sialic acid from transferrin. The interpretation is presented that the faint components may represent the absence of multi-unit carbohydrate prosthetic groups on the transferrin molecule in the infant. A similar interpretation is possible for the slow migrating transferrins of cerebrospinal fluid.

Blood Protein Electrophoresis↗
PubMed1962

Additional genetic variation of human serum transferrin.

A new molecular species of human transferrin, Tf $$Word$$, is described. Starch gel electrophoresis under high-voltage conditions permits the new variant to be clearly distinguished from previously described variants of closely similar mobilities. The presence of a faint iron-binding component which migrates slightly more rapidly than the principal transferrin with which it is associated is also described.

Electrophoresis↗
PubMed1962

Studies on the transferrins of adult serum, cord serum, and cerebrospinal fluid. The effect of neuraminidase.

Nine of the twelve known variants of human transferrin have been resolved by the action of neuraminidase into stepwise patterns of four additional slower moving components whose relative intensities depended upon the concentration of enzyme. These components appeared to represent the stepwise removal of the four sialic acid residues from the transferrin molecule, and at large enzyme concentrations, almost all of the transferrin was reduced to the position of the slowest moving component. In contrast, the electrophoretic mobilities of haptoglobin, ceruloplasmin, and alpha(2)-macroglobulin showed a gradual decrease with increasing neuraminidase concentration. The transferrins of chimpanzees, rhesus and cynomolgus monkeys, and cattle were resolved by neuraminidase into two slower moving components. These experiments suggested that the primate and cattle transferrins contained only two sialic acid residues accessible to the enzyme. Transferrins C, B(2), and D(1) and a cynomolgus monkey transferrin were purified from serum by starch block electrophoresis and cellulose chromatography. Ultracentrifugal analysis could detect no difference in sedimentation rate between transferrin C, the primate transferrin, and neuraminidase-treated transferrin C. The human transferrins showed no variation in amino acid composition, but the cynomolgus transferrin was approximately 20 per cent higher in serine content and 50 per cent lower in glucosamine than human transferrin C. Reactions of antigenic identity were obtained among five human transferrin variants but a reaction of only partial identity was obtained between transferrin C and the cynomolgus transferrin. The transferrin pattern of cord blood showed a prominent band in the position of transferrin C, accompanied by four faint slower moving bands which coincided with the four transferrin components produced by the action of neuraminidase on transferrin C. The transferrin pattern of cerebrospinal fluid in individuals homozygous for serum transferrin C showed two principal components, one of which appeared to contain no sialic acid. Haptoglobin, ceruloplasmin, and alpha(2)-macroglobulin were also present in cerebrospinal fluid.

Adult↗
PubMed1961

Alterations in sialic acid content of human transferrin.

Starch gel electrophoresis of human transferrin treated with neuraminidase revealed a pattern of five bands whose intensities varied with neuraminidase concentration. Sialic acid analysis after starch block electrophoresis suggested that the bands represented the stepwise removal of sialic acid from the transferrin molecule. Evidence was also obtained for the purification of a particular genetic transferrin variant

Humans↗