Hemoglobin deer lodge: α2β2 2 His → Arg

Labossiere, A.; Vella, F.; Hiebert, John M.; Galbraith, P.A.

doi:10.1016/s0009-9120(72)80007-9

Cited by 45 publications

(8 citation statements)

References 11 publications

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“…(23,24) that also results in an NH2-terminal elongated chain owing to the preservation of the initiator methionine. In contrast, the other known variants at the (2 site, Hb Deer Lodge (His Arg) (25) and Hb Okayama (His -> Gln) (26) (28). Na-acetyltransferases have been discovered in a variety of tissues (28)(29)(30)(31)(32) and do not display either cellular or phylogenetic specificity.…”

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confidence: 99%

Amino-terminal processing of proteins: hemoglobin South Florida, a variant with retention of initiator methionine and N alpha-acetylation.

Boissel¹,

Kasper²,

Shah³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

106

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The hemoglobin variant South Florida has been shown by protein sequencing and fast-atom-bombardment mass spectroscopy to have a substitution ofmethionine for the NH2-terminal valine of the (8-globin chain. In addition, there was complete retention of the initiator methionine on the mutant polypeptide. Approximately 20% of the protein was acetylated at the NH2 terminus of the (3 chain. A search of a comprehensive data bank of protein and gene sequences revealed 84 unrelated vertebrate proteins that have not undergone cleavage of leader sequences. A highly nonrandom distribution of residues at the NH2 termini of these proteins predicts removal of the initiator methionine as well as NH2-terminal acetylation. Proteins that undergo removal commonly have serine, alanine, glycine, or valine, as the NH2-terminal residues. The first three residues favor N-acetylation. Proteins that retain the initiator methionine commonly have a charged residue or methionine at the second position. Information on Hb South Florida and other hemoglobins coupled with this survey of primary sequence provides insights into the NH2-terminal processing of proteins.The biological properties of a large number of proteins are significantly altered by cotranslational and posttranslational modifications. In eukaryotes, the initiation of translation takes place at an AUG codon on mRNA (1). The NH2-terminal methionine residue is generally cleaved from the nascent polypeptide by an aminopeptidase (2). Soon thereafter the new NH2-terminal residue is often acetylated at the a-amino group (3,4). Only fragmentary information on NH2-terminal processing is available and, therefore, the molecular mechanism is still poorly understood. It has been suggested that cleavage of the initiator methionine is prevented when the adjacent residue is a charged amino acid (5). The MATERIALS AND METHODSPhosphate-free hemolysates (6) were prepared from heparinized blood samples. Hemolysate (1-2 g of hemoglobin) was analyzed on a column (5 x 22 cm) of Bio-Rex 70 (Bio-Rad) cation-exchange resin as described (7). The "Hb Al," fraction was dialyzed vs. 0.25 M ammonium acetate, pH 8.5, and rechromatographed on a column (2 x 6 cm) of Glycogel B boronate affinity resin (Pierce) (8). The non-retained Hb fraction from the affinity column and Hb A0 fraction from Bio-Rex chromatography were converted to globin by acid/acetone precipitation (9) and separated into a and /3 subunits by carboxymethyl-cellulose chromatography in 8 M urea. After aminoethylation (10), the isolated chains were digested with trypsin (11 Tryptic peptides were dissolved in 0.5% acetic acid/glycerol, 1:1 (vol/vol) solution. About 2 ,ug of the sample was applied per analysis.Abbreviations: FAB-MS, fast-atom-bombardment mass spectroscopy; RP-HPLC, reverse-phase HPLC. 8448The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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confidence: 99%

Amino-terminal processing of proteins: hemoglobin South Florida, a variant with retention of initiator methionine and N alpha-acetylation.

Boissel¹,

Kasper²,

Shah³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

106

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“…So far, Hb Graz has been found in four unrelated patients and their families [20]. Hb Graz is the second hemoglobin variant detected in Austria and represents the fourth hemoglobin variant with a mutation in the second codon of the beta chain [8][9][10]. Consanguinity based on family history seems unlikely, although a founder effect cannot be completely excluded.…”

Section: Discussionmentioning

confidence: 93%

“…Another family with Hb Graz living in K6flach, Styria, was found by the authors in 1995. In addition to the slightly unstable Hb Campertown, oz2/32104(G6)Arg~Ser [22], Hb Sherwood Forest is the second hemoglobin variant found with a mutation in position 104 of the /3-chain [10]. We estimate the prevalence in our diabetic population now at 0.45%o, based on 11000 diabetic patients who had HbA~c determination over a period of 5 years.…”

Section: Discussionmentioning

confidence: 99%

Hemoglobin variants recently detected in Austria

et al. 1995

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Measurement of glycated hemoglobin (HbAtc) is used for routine management of diabetic patients. Glucose linkage to HbAtc reflects mean blood glucose levels during the last 3 months before examination. Various methods for HbA1c determination show abnormal values with hemoglobin variants. In some diabetic patients excessively high HbA1c values with high-performance liquid chromatography (HPLC) led to the detection of Hb Graz. In addition to Hb Graz, other silent hemoglobin variants have been found in Austria. Here we review Hb Graz, Hb Sherwood Forest, and Hb Okayama detected while using HPLC for the measurement of HbA1c in diabetic patients.

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“…It is Hb Deer Lodge (f32 His + Arg) [12]. Like Hb Okayama this variant showed an increased oxygen affinity, but no clinical signs [12,13].…”

Section: Discussionmentioning

confidence: 94%

Hemoglobin Okayama [β‐2 (NA 2) His → Gln]: A new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3‐diphosphoglycerate binding site

Harano

Shibata

et al. 1983

FEBS Letters

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A new 'silent' abnormal hemoglobin, Hb Okayama IB2 (NA 2) His + Gln], happened to be discovered in a diabetic Japanese female living in Okayama Prefecture, Japan, in the course of glyco-Hb measurement of the blood samples of diabetic patients. This variant did not differ from Hb A by conventional electrophoretic tests. Only the isoelectric focusing on PAG plate for the determination of glyco-Hb and the cation exchanger chromatography were successful in the separation of this abnormal variant from Hb A and glyco-Hb. Functional study of the whole blood demonstrated a slight increase of oxygen affinity. Hb Okayama 682 (NA 2) His + Gln]Silent Hb variant

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Hemoglobin deer lodge: α2β2 2 His → Arg

Cited by 45 publications

References 11 publications

Amino-terminal processing of proteins: hemoglobin South Florida, a variant with retention of initiator methionine and N alpha-acetylation.

Amino-terminal processing of proteins: hemoglobin South Florida, a variant with retention of initiator methionine and N alpha-acetylation.

Hemoglobin variants recently detected in Austria

Hemoglobin Okayama [β‐2 (NA 2) His → Gln]: A new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3‐diphosphoglycerate binding site

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