The Hemoglobins

Braunitzer, Gerhard; Hilse, Kurt; Rudloff, Victor; Hilschmann, Norbert

doi:10.1016/s0065-3233(08)60188-6

Cited by 172 publications

(37 citation statements)

References 211 publications

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“…determined by silica-gel thin layer chromatography (16) and automatic amino acid analysis (17 Oxygen equilibria determined by oxygen electrode and continuous recording spectrophotometry of Hb Hiroshima showed characteristics almost identical with those for suspensions and hemolysates described above. shows curves for purified Hb Hiroshima and an hemolysate from another carrier (III3) compared with Hb A.…”

Section: Methodssupporting

confidence: 56%

Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Hamilton¹,

Iuchi²,

Miyaji³

et al. 1969

J. Clin. Invest.

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Section: Methodssupporting

confidence: 56%

Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Hamilton¹,

Iuchi²,

Miyaji³

et al. 1969

J. Clin. Invest.

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“…Hemoglobin A has three pairs of cysteine residues. Each a-chain has one cysteine at position 104, while the f-chains have residues at positions 93 and 112 (32). The P93 cysteines are situated at the surface of the hemoglobin tetramer, while the P112 and a104 cysteines are in the interior of the molecule at the ap, contact (33).…”

Section: Methodsmentioning

confidence: 99%

“…The tyrosine in hemoglobin A is at position 35 of the p-chain, counting from the amino terminal end, and occupies position number one in the C helix. (32,33). Hemoglobin Philly can therefore be designated as #35 (Cl) tyrosine -* phenylalanine.…”

Section: )mentioning

confidence: 99%

Hemoglobin Philly (β35 tyrosine→phenylalanine): studies in the molecular pathology of hemoglobin

Rieder¹,

Oski²,

Clegg³

1969

J. Clin. Invest.

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“…Failure to detect identical tryptic peptides in different polypeptide chains is by no means evidence against evolutionary relatedness; the a and /3 chains of human hemoglobin, which are identical in 40% of their residues (26), have no tryptic products in common except free lysine (27 …”

mentioning

confidence: 99%

Covalent structure of subunits of bacterial luciferase: NH2-terminal sequence demonstrates subunit homology.

Baldwin¹,

Ziegler²,

Powers³

1979

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

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The heterodimeric subunit structure of bacterial luciferase was'demonstrated more than 10 years ago. The enzymes from both Beneckea harveyi and Photobacterium fischeri have since been studied in detail; they each consist of two nonidentical subunits, designated a and f. Both are required for bioluminescence activity, with the active center apparently confined to the a subunit. Amino acid sequence analysis-of the NH2 termini of the a and P subunits of the B. harveyi and P. fischeri luciferases not only confirms the earlier observation that the a subunits are homologous but also demonstrates that the NHrterminal sequences of the P subunits-of the luciferases from the-two genera are homologous. Furthermore, within each luciferase, the NHrterminal sequences of the a and 13 subunits are similar, suggesting the possibility that the genes coding for a and ft may have arisen by gene duplication, presumably prior to divergence of the lines leading to present-day luminous bacteria.Bacterial luciferase catalyzes the mixed function oxidation of reduced flavin mononucleotide (FMNHI2) and a long-chain saturated aldehyde to yield the corresponding carboxylic acid, oxidized flavin, and blue-green light (Xmaha t490 nm) (2). The enzyme is a heterodimer (a/3) with subunit molecular weights obtained from electrophoresis in sodium dodecyl sulfate of 42,000 and 37,000 for Beneckea harveys a and 3, respectively, and 41,000 and 38,000 for the corresponding Photobacteorum fischeri subunits (3) ¶1-The structural nonidentity of the luciferase a'and 3 subunits was first demonstrated clearly by separation of the subunits on columns of DEAE-cellulose in urea-containing buffers (5) and by electrophoretic resolution in polyacrylamide gels containing urea or sodium dodecyl sulfate (3). The a''and /3 subunits have been shown to have different amino acid compositions (3) and tryptic peptide maps (4). However, the discovery of three identical tryptic peptides between the higher molecular weight subunits, from the P. fischeri and B. harveyi luciferases suggested that the a subunits of the luciferases from these two genera are homologous (4).The functional nonidentity of the luciferase a and /3 subunits was first demonstrated by chemical modification of the enzyme (6, 7) and has been confirmed by mutant enzyme analysis (8), additional chemical modification studies (9, 10), differences in susceptibility to proteases (11), and numerous ligand binding studies (12)(13)(14)(15)(16)(17). The enzyme has a single flavin-binding site. The binding of reduced flavin has been demonstrated by using a kinetic technique (12), fluorescence quenching (13), and circular dichroism (14). The binding of oxidized flavin has been demonstrated by equilibrium dialysis (15) (14).The rather compelling conclusion drawn from all of these observations is that the luciferase a and /3 subunits are quite distinct, both structurally and functionally. We

show abstract

The Hemoglobins

Cited by 172 publications

References 211 publications

Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Hemoglobin Hiroshima (β143 histidine → aspartic acid): a newly identified fast moving beta chain variant associated with increased oxygen affinity and compensatory erythremia

Hemoglobin Philly (β35 tyrosine→phenylalanine): studies in the molecular pathology of hemoglobin

Covalent structure of subunits of bacterial luciferase: NH2-terminal sequence demonstrates subunit homology.

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