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Biomedical subjects

A G BEARN

Publications and source records attributed to A G BEARN.

At least 19 recordsLinked to original sources
PubMed1964

HEREDITARY DEFICIENCY OF SERUM ALPHA-L-ANTITRYPSIN.

Deficiency of the serum alpha(1),-antitrypsin appears to be under genetic control. The level of this protein is reduced to less than 10 percent of the norm in individuals homozygous for the trait, who may suffer from pulmonary emphysema. Heterozygous individuals have a concentration of serum alpha(1)-antitrypsin between 50 and 60 percent of normal, but appear to be in good health. The estimated heterozygous frequency of the trait in a small white population in Georgia is 2.1 percent.

Blood Protein Disorders↗
PubMed1964

IMMUNOLOGICAL AND BIOCHEMICAL STUDIES ON SERUM HAPTOGLOBIN.

Antibody to purified type 1-1 human serum haptoglobin was obtained in rabbits. Using this antiserum it was demonstrated that the antigenic determinants of the haptoglobin molecule reside in both alpha- and beta-chains. No immunological difference between the normal alpha(1F)- and alpha(1S)-chains of haptoglobin could be detected. A number of healthy individuals whose haptoglobin pattern appeared normal by starch gel electrophoresis were shown to possess a haptoglobin which could be distinguished immunologically from the common haptoglobin types. These immunological atypical haptoglobins have been observed in individuals of types 1-1, 2-1, and 2-2. Combined immunological and chemical studies of purified haptoglobin have enabled the construction of a tentative model for the structure of human type 1-1 haptoglobin.

Animals↗
PubMed1964

HETEROGENEITY OF THE INHERITED GROUP-SPECIFIC COMPONENT OF HUMAN SERUM.

Heterogeneity of the group-specific (Gc) components in normal human serum has been demonstrated by the use of a lithium borate buffer system in conventional vertical starch gel electrophoresis and by prolonged immunoelectrophoresis in agar gel. In both Gc 1-1 and Gc 2-2 phenotypes a protein component migrates ahead of the main band. Immunological evidence indicates that the faster migrating band contains Gc specificity. The possibility that the two electrophoretically distinct Gc components share a common polypeptide chain is discussed.

Blood Group Antigens↗
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↗
PubMed1963

ISOLATION AND PARTIAL CHARACTERIZATION OF THE TWO PRINCIPAL INHERITED GROUP-SPECIFIC COMPONENTS OF HUMAN SERUM.

The group-specific component (Gc), an alpha(2)-globulin of human plasma with inherited variations in relative electrophoretic mobility, has been isolated from plasma and partially characterized. The isolation procedure combines ammonium sulfate fractionation, anion exchange chromatography, preparative zone electrophoresis, and gel filtration. The method is suitable for the isolation and purification of the group-specific components. The Gc proteins representing the gene products of the two common homozygous Gc-types) Gc 1-1 and Gc 2-2, have been prepared. Gc belongs to the group of alpha(2)-globulins of relatively low molecular weight (4.1S, molecular weight 50,800) and relatively low carbohydrate content (3.3 per cent). The total amino acid composition of the two homozygous group-specific components is very similar; treatment with reducing agents and alkylation provides no evidence for the presence of more than a single polypeptide chain in the Gc molecule.

Amino Acids↗