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Biomedical subjects

R D Koler

Publications and source records attributed to R D Koler.

53 records · Page 3Linked to original sources
PubMed1969

Ontogeny of soluble and mitochondrial tyrosine aminotransferases.

The development of the soluble and mitochondrial forms of tyrosine aminotransferase was observed in fetal and neonatal rhesus monkey tissues. The mitochondrial activity is detectable in early fetal life; the soluble form reaches significant activity just before the birth of the animal.

Aging↗
PubMed1967

Hemoglobin Yakina. I. Clinical and biochemical studies.

Three members of a family who have erythrocytosis and a new hemoglobin, designated hemoglobin Yakima, are described. The abnormal hemoglobin is characterized by the substitution of histidine for aspartic acid at residue 99 in the beta-chain. Of three possible structure-function relations which would account for the increased oxygen affinity of hemoglobin Yakima, only two seem likely. These are: (a) an intrachain shift in the normal relations between the F and G helices and the heme group, or (b) an effect of the substituted side chain at a region of contact between nonpolar residues of the alpha- and beta-chains which favors the oxyhemoglobin quarternary structure.

Aspartic Acid↗
PubMedDate not supplied

Hemoglobin Willamette (alpha2beta2 51Pro replaced by Apg (D2)) a new abnormal human hemoglobin.

A hemoglobin variant with the same electrophoretic mobility as hemoglobin S was found in three generations of a black family. No clinical symptoms or findings were present in subjects heterozygous for this mutant. Except for target forms of mature erythrocytes, they have no abnormal hematologic findings. Structural studies demonstrated a previously undescribed substitution, beta51 Pro replaced by Arg, in the abnormal fraction which accounts for about one-third of the total hemoglobin. This fraction is more unstable in vitro at 65 degrees than normal A hemoglobin. Both whole blood and purified abnormal hemoglobin have increased oxygen affinity and a slightly decreased Bohr effect.

Arginine↗