Literature DB >> 4639808

High resolution proton magnetic resonance study of the two quaternary states in fully ligated hemoglobin Kansas.

S Ogawa, A Mayer, R G Shulman.   

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Year:  1972        PMID： 4639808     DOI： 10.1016/0006-291x(72)90507-4

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  5 in total

1.  Magnitude of subunit inequivalence for oxygen release from hemoglobin: reinvestigation of the oxygen-pulse experiment.

Authors:  J M Salhany; C L Castillo; M J McDonald; Q H Gibson
Journal:  Proc Natl Acad Sci U S A       Date:  1975-10       Impact factor: 11.205

2.  Structure-function relations in hemoglobin as determined by x-ray absorption spectroscopy.

Authors:  P Eisenberger; R G Shulman; G S Brown; S Ogawa
Journal:  Proc Natl Acad Sci U S A       Date:  1976-02       Impact factor: 11.205

3.  Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin.

Authors:  J M Salhany; S Ogawa; R G Shulman
Journal:  Proc Natl Acad Sci U S A       Date:  1974-09       Impact factor: 11.205

4.  A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.

Authors:  S Takahashi; A K Lin; C Ho
Journal:  Biophys J       Date:  1982-07       Impact factor: 4.033

5.  A recombinant human hemoglobin with asparagine-102(beta) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride.

Authors:  H Yanase; L R Manning; K Vandegriff; R M Winslow; J M Manning
Journal:  Protein Sci       Date:  1995-01       Impact factor: 6.725
  5 in total

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