Literature DB >> 3390144

1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin.

H S Aojula1, M T Wilson, G R Moore, D J Williamson.   

Abstract

1H-n.m.r. and c.d. studies on sperm-whale myoglobin show that the c.d. signal in the Soret region is inversely and linearly related to the proportion of minor isomer present. An alternative method, 'pH jump', is described for inducing orientational disorder in sperm-whale myoglobin without recourse to reconstitution. 1H-n.m.r. studies on human haemoglobin A indicate little heterogeneity in freshly isolated haemoglobin A, but the effect is enhanced in freeze-dried Sigma haemoglobin A.

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Year:  1988        PMID: 3390144      PMCID: PMC1148933          DOI: 10.1042/bj2500853

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  17 in total

1.  Cleavage of the haem-protein link by acid methylethylketone.

Authors:  F W TEALE
Journal:  Biochim Biophys Acta       Date:  1959-10

2.  Optical rotatory dispersion of a respiratory hemeprotein of Chironomus thummi.

Authors:  H Formanek; J Engel
Journal:  Biochim Biophys Acta       Date:  1968-06-26

3.  Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy.

Authors:  T Jue; G N La Mar
Journal:  Biochem Biophys Res Commun       Date:  1984-03-15       Impact factor: 3.575

4.  Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein.

Authors:  G N La Mar; N L Davis; D W Parish; K M Smith
Journal:  J Mol Biol       Date:  1983-08-25       Impact factor: 5.469

5.  Proton nuclear nagnetic resonance characterization of heme disorder in monomeric insect hemoglobins.

Authors:  G N La Mar; K M Smith; K Gersonde; H Sick; M Overkamp
Journal:  J Biol Chem       Date:  1980-01-10       Impact factor: 5.157

6.  Preparation and properties of apohemoglobin and reconstituted hemoglobins.

Authors:  F Ascoli; M R Fanelli; E Antonini
Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

7.  Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effects.

Authors:  J T Lecomte; R D Johnson; G N La Mar
Journal:  Biochim Biophys Acta       Date:  1985-06-10

8.  1H NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin.

Authors:  G N La Mar; Y Yamamoto; T Jue; K M Smith; R K Pandey
Journal:  Biochemistry       Date:  1985-07-16       Impact factor: 3.162

9.  Haem disorder in reconstituted human haemoglobin.

Authors:  J C Docherty; S B Brown
Journal:  Biochem J       Date:  1982-12-01       Impact factor: 3.857

10.  Haem disorder in modified myoglobins. Effect of reconstitution procedures.

Authors:  M B Ahmad; J R Kincaid
Journal:  Biochem J       Date:  1983-10-01       Impact factor: 3.857

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  4 in total

1.  Haem disorder in recombinant- and reticulocyte-derived haemoglobins: evidence for stereoselective haem insertion in eukaryotes.

Authors:  A J Mathews; T Brittain
Journal:  Biochem J       Date:  2001-07-01       Impact factor: 3.857

2.  Expression in Escherichia coli of the flavin and the haem domains of Hansenula anomala flavocytochrome b2 (flavodehydrogenase and b2 core) and characterization of the recombinant proteins.

Authors:  M C Silvestrini; M Tegoni; J Célerier; A Desbois; M Gervais
Journal:  Biochem J       Date:  1993-10-15       Impact factor: 3.857

3.  Kinetic and spectroscopic studies of haemoglobin and myoglobin from Urechis caupo. Distal residue effects.

Authors:  T J DiFeo; A W Addison; J J Stephanos
Journal:  Biochem J       Date:  1990-08-01       Impact factor: 3.857

4.  Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins.

Authors:  T J DiFeo; A W Addison
Journal:  Biochem J       Date:  1989-06-15       Impact factor: 3.857

  4 in total

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