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Biomedical subjects

J B Wilson

Publications and source records attributed to J B Wilson.

At least 199 records · Page 11Linked to original sources

Hb J-Singa (alpha-78 Asn leads to Asp), a newly discovered hemoglobin variant with the same amino acid substitution as one of the two present in Hb J-Singapore (alpha-78 Asn leads to, alpha-79 Ala leads to Gly).

A new fast-moving alpha-chain Hb variant with an Asn leads to Asp substitution at position alpha-78 was found in a French-Acadian family living in Eastern Canada. The identical substitution was reported in Hb J-Singapore, which also had an additional Ala leads to Gly substitution at position alpha-79. The new variant, which did not result in any clinical symptoms, was named accordingly, Hb J-Singa.

Adult↗

Hemoglobin Hamilton or alpha 2 beta 2 11(A8)Val leads to Ile: a silent beta-chain variant detected by Triton X-100 acid-urea polyacrylamide gel electrophoresis.

A silent beta-chain hemoglobin variant, not detectable by starch gel or agar gel electrophoresis was found using Triton X-100 acid-urea polyacrylamide gel electrophoresis. The abnormal beta-X chain had a more anodic electrophoretic mobility; 38% of the total beta chain was of the abnormal type. Structural analysis using high-performance liquid chromatography and microsequencing procedures indicated a valine to isoleucine substitution at position beta 11(A8). This anomaly did not change the functional properties of the hemoglobin molecule. A mild reticulocytosis was observed in the propositus.

Electrophoresis, Polyacrylamide Gel↗

Quantitation of hemoglobin components by high-performance cation-exchange liquid chromatography: its use in diagnosis and in the assessment of cellular distribution of hemoglobin variants.

Additional data are presented that were obtained with a newly developed cation-exchange high-performance liquid chromatography (HPLC) method allowing the separation of numerous normal and abnormal human hemoglobin types. The method was found to be of considerable value for the diagnosis of certain hemoglobinopathies in the adult as well as in the newborn. Definitive differentiation between, AS, SS, S-beta+-thal, SD, SC, AC, C-beta+-thal, etc in cord bloods was readily accomplished even when the samples were collected on filter paper. Analyses of the hemoglobin in cells from Hb S and Hb C heterozygotes with different numbers of alpha chain genes (alpha alpha/alpha alpha; -alpha/alpha alpha; -alpha/-alpha) after separation by a Dextran density centrifugation technique failed to show significant changes in the relative quantitation of the variant hemoglobin types. Glycosylation of hemoglobin increased greatly with an increase in red cell age. Similar analyses of red cells from a young girl with Hb S trait and Hb H disease (the --/-alpha genic arrangement) gave comparable data. Some indication was obtained that her youngest cells contained some of the beta A4 and beta S4 tetrameric hemoglobins.

Adult↗

The characterization of hemoglobin Manitoba or alpha (2)102(G9)Ser----Arg beta 2 and hemoglobin Contaldo or alpha (2)103(G10)His----Arg beta 2 by high performance liquid chromatography.

Hb Contaldo with a His----Arg substitution at position 103(G10) of the alpha chain is a newly discovered unstable Hb variant observed in an Italian child. Its instability is probably due to the disruption of the hydrogen bond between alpha 103(G10)His and beta 108(G10)Asn. The structural variation in the core segment was determined through analysis of tryptic peptides from digests of the alpha X and oxidized alpha X (with performic acid) chains, which were separated by HPLC. Similar analyses were made for the alpha X chain of the rare Hb Manitoba in which alpha 102(G9) Ser is replaced by Arg. This variant was observed for the first time in an Italian patient, and was also studied in a member of a previously described Canadian family.

Amino Acids↗