Bernadine Brimhall

Hemoglobin Yakima: 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 8l-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 a- and fl-chains which favors the oxyhemoglobin quarternary structure.

Hemoglobin Freiburg: Abnormal Hemoglobin due to deletion of a Single Amino Acid Residue.

Structural characterization of a new variant of human hemoglobin (adult), designated hemoglobin Freiburg, indicates the deletion of the valyl residue No. 23 from an otherwise normal beta-chain. The formula may be written α2β223val—0. The abnormal hemoglobin is present with hemoglobin A in the proposita and in two of her three living children, but is not detectable in her parents. We postulate that this variant represents a triplet base deletion which most likely resulted from an unequal crossing-over between two normal betachain loci during meiosis in one of the parents of the proposita.

Hemoglobin sabine beta 91 (f 7) leu to pro. An unstable variant causing severe anemia with inclusion bodies.

Abstract Hemoglobin Sabine (α2β2 91 leu → pro) comprises 8 per cent of the hemoglobin of a 16-year-old Scotch-English-German girl who has suffered from hemolytic anemia since infancy. The spleen wa...

Chemical characterization of hemoglobinMexico and hemoglobinChiapas

Two new hemoglobins found during surveys of several Indian populations in Mexico have been chemically characterized. The first, HbMexico, was found in two unrelated individuals and was shown to be α254Gln→Glu β2. The second, HbChiapas, was found to have the structure α2114Pro→Argβ2.

Two new hemoglobins: Hemoglobin Alabama [β39(C5)Gln → Lys] and hemoglobin Montgomery [α48(CD6)Leu → Arg]

Abstract The amino acid substitutions in two new hemoglobins found by electrophoretic screening during a survey in Alabama have been determined by column chromatography and amino acid analyses of their tryptic peptides. They are hemoglobin Alabama [β 39(C 5)Gln → Lys] and hemoglobin Montgomery [α 48(CD 6)Leu → Arg]. No harmful symptoms have been attributed to the presence of either hemoglobin.

The amino acid sequence of dog (Canis familiaris) hemoglobin.

SummaryThe manual sequencing of the tryptic peptides from theα andβ chains of dog hemoglobin is described, including evidence for the existence of twoαT-13 peptides and thus 2α chains, one with threonine and one with alanine at position 130. Although the actual sequence was published in 1970, the evidence on which it was based has not previously appeared.

Structural characterizations of hemoglobins J-Buda [α 61 (E 10) Lys→Asn] and G-pest [α 74 (EF 3) Asp→Asn]

Abstract Two new mutant hemoglobins, each with abnormal α-chains, have been found along with normal adult hemoglobin in three brothers of a Hungarian family. Preliminary identification of the abnormal chains and genetic studies have been reported earlier (Hollan, S. R., Szelenyi, J. G., Brimhall, B., Duerst, M., Jones, R. T. Koler, R. D. and Stocklen, Z. (1972) Nature 235, 47–50). The present paper reports the structural characterizations of the two abnormal α-chains found in affected members of this family and of the normal α-chain from one of the brothers who also had the two abnormal hemoglobins. One abnormal hemoglobin, named J-Buda, has a substitution of an asparaginyl residue for the lysyl residue 61 (E 10) of its α-chain. The second abnormal hemoglobin, named G-Pest, has an asparaginyl residue for the aspartyl residue 74 (EF 3) of its α-chain. The amino acid compositions of all of the other tryptic peptides of the abnormal α-chains and of all of the tryptic peptides of the normal α-chain from one of the affected brothers were identical to compositions reported for tryptic peptides of normal human α-chains. We conclude that except for the substitution of single amino acid residues in the two abnormal α-chains, the compositions and probably the sequences of amino acid residues of the four gene products from two α-chain loci are identical, at least in this Hungarian family.

Haemoglobin F Jamaica (α2γ261 Lys→Glu; 136 Ala)

Summary. Two siblings of mixed Negro, East Indian and Caucasian parentage showed an abnormal haemoglobin component in infancy which had electrophoretic characteristics similar to Hb F Roma (Silvestroni & Bianco, 1963). The amino‐acid substitution responsible for the peculiar electrophoretic mobility was found to be in the gamma polypeptide chain (γ— 61(E5) Lys→Glu). The finding of an alanyl residue at position 136 of the γ‐chain of the abnormal component in the first born of these infants was repeated in the abnormal γ‐chain of the second infant. No functional abnormalities were found to be associated with this abnormal haemoglobin, which is designated Hb F Jamaica.

The tryptic peptide composition of the beta chains of hemoglobins A and B of the Domestic cat (Felis catus)

SummaryThe tryptic peptides from theβA andβB chains of cat hemoglobins A and B have been isolated and the amino acid compositions determined. Differences between the two chains were found in two peptides,βT-1 (Gly→Ser) andβT-14 (Asn→Ser and Lys→Arg). The Gly→Ser and Lys→Arg substitutions are placed atβ-1 andβ-144 respectively from earlier work, and the third substitution, Asn→Ser atβ-139 is suggested from this work. In addition, the presence of a blocked amino terminus inβB has been confirmed. Tentative sequences constructed by homology with knownβ-chain structures suggest the occurrence of substitutions atα1β1 contacts inβA andβB that may be functionally significant. There are at least 18 differences in amino acid composition between catβA and dogβ-chains and 22 differences between catβA and normal adult humanβ-chains.

A variant present in unusually low concentration

Hb Ft. Worth, α27Glu → Gly(B8), constitutes about 5% of the hemoglobin of two members of a Negro family, both of whom exhibit slight hypochromia and microcytosis.