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Modification of hemoglobin with site-directed bifunctional reagents
M. P. Kavanaugh
, D. T.B. Shih
, R. T. Jones
Division of Biological and Biomedical Sciences
Center for Structural and Functional Neuroscience
Center for Translational Medicine
Oregon Health and Science University
Research output
:
Contribution to journal
›
Article
›
peer-review
5
Scopus citations
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Biochemistry, Genetics and Molecular Biology
Oxygen Affinity
100%
Adenosine Triphosphate
100%
Nicotinamide Adenine Dinucleotide
100%
Phosphoribosyl Pyrophosphate
100%
Cross-Link
50%
Glucose 1-Phosphate
50%
Periodate
50%
Binding Site
50%
Nicotinamide Adenine Dinucleotide Phosphate
50%
Phytic Acid
50%
Polyacrylamide Gel Electrophoresis
50%
Lead Phosphate
50%
Pharmacology, Toxicology and Pharmaceutical Science
Phosphoribosyl Pyrophosphate
100%
Adenosine Triphosphate
100%
Nicotinamide Adenine Dinucleotide
100%
Phytic Acid
50%
Glucose 1 Phosphate
50%
Periodate
50%
Blood Substitute
50%
Binding Site
50%
Nicotinamide Adenine Dinucleotide Phosphate
50%
Polyacrylamide Gel Electrophoresis
50%
Organophosphate
50%
Chemistry
ATP
100%
formation
100%
Nicotinamide Adenine Dinucleotide
100%
NADP
50%
SDS Polyacrylamide Gel Electrophoresis
50%
Binding Site
50%
Organic Phosphate
50%
Blood Substitute
50%
Periodate
50%
Inositol
50%
Lead Phosphate
50%