Carbon-13 NMR studies of C2H5N13C bound to hemoproteins — Evidence for a different distal proteic environment in β-chains either isolated or within human hemoglobin-Reference-Cited by-同舟云学术

Carbon-13 NMR studies of C2H5N13C bound to hemoproteins — Evidence for a different distal proteic environment in β-chains either isolated or within human hemoglobin

Published:1978-07 Issue:1 Volume:83 Page:217-225
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Mansuy D.,Thillet J.,Cendrier B.,Lallemand J.Y.,Chottard J.C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference32 articles.

1. Carbon-13 NMR studies of C2H5N13C binding to various hemoproteins

2. Natural abundance 13 C spectra of proteins: Carboxy-myoglobin and hemoglobin

3. Nuclear magnetic resonance studies of carbon-13 monoxide binding to various hemoglobins

4. Carbon-13 NMR studies of 13Co binding to human hemoglobin

5. Carbon-13 nuclear magnetic resonance and infrared spectroscopic studies of carbon-13 monoxide binding to rabbit hemoglobin

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