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Biochemistry
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December 22, 1992
Amadori rearrangement potential of hemoglobin at its glycation sites is dependent on the three-dimensional structure of protein
P Nacharaju, A S Acharya
Biochemistry
|
August 27, 1985
Reactivity of Glu-22(beta) of hemoglobin S for amidation with glucosamine
A S Acharya, R Seetharam
Journal of Protein Chemistry
|
April 1, 1989
Selective amidation of carboxyl groups of the intermolecular contact regions of hemoglobin S: structural aspects
A S Acharya, L Khandke
Molecular and Cellular Biochemistry
|
May 14, 1982
Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation
A S Acharya, H Taniuchi
Proceedings of the National Academy of Sciences of the United States of America
|
June 1, 1977
Formation of the four isomers of hen egg white lysozyme containing three negative disulfide bonds and one open disulfide bond
A S Acharya, H Taniuchi
Journal of Cellular Biochemistry
|
January 1, 1986
Synthetic potential of Staphylococcus aureus V8-protease: an approach toward semisynthesis of covalent analogs of alpha-chain of hemoglobin S
R Seetharam, A S Acharya
Biophysical Journal
|
May 12, 2009
On the renaturation of reduced hen egg white lysozyme containing two blocked sulfhydryl groups
A S Acharya, H Taniuchi
Biochemistry
|
July 25, 1978
Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127
A S Acharya, H Taniuchi
International Journal of Peptide and Protein Research
|
May 1, 1980
Preparation of a two-disulfide bonded enzymically active derivative from hen egg lysozyme
A S Acharya, H Taniuchi
The Journal of Biological Chemistry
|
November 25, 1976
A study of renaturation of reduced hen egg white lysozyme. Enzymically active intermediates formed during oxidation of the reduced protein
A S Acharya, H Taniuchi
Page
of 9
Search research articles
Search
Showing results (1-10 of 89) with videos related to
Sort By:
Page
of 9
Biochemistry
|
December 22, 1992
Amadori rearrangement potential of hemoglobin at its glycation sites is dependent on the three-dimensional structure of protein
P Nacharaju, A S Acharya
Biochemistry
|
August 27, 1985
Reactivity of Glu-22(beta) of hemoglobin S for amidation with glucosamine
A S Acharya, R Seetharam
Journal of Protein Chemistry
|
April 1, 1989
Selective amidation of carboxyl groups of the intermolecular contact regions of hemoglobin S: structural aspects
A S Acharya, L Khandke
Molecular and Cellular Biochemistry
|
May 14, 1982
Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation
A S Acharya, H Taniuchi
Proceedings of the National Academy of Sciences of the United States of America
|
June 1, 1977
Formation of the four isomers of hen egg white lysozyme containing three negative disulfide bonds and one open disulfide bond
A S Acharya, H Taniuchi
Journal of Cellular Biochemistry
|
January 1, 1986
Synthetic potential of Staphylococcus aureus V8-protease: an approach toward semisynthesis of covalent analogs of alpha-chain of hemoglobin S
R Seetharam, A S Acharya
Biophysical Journal
|
May 12, 2009
On the renaturation of reduced hen egg white lysozyme containing two blocked sulfhydryl groups
A S Acharya, H Taniuchi
Biochemistry
|
July 25, 1978
Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127
A S Acharya, H Taniuchi
International Journal of Peptide and Protein Research
|
May 1, 1980
Preparation of a two-disulfide bonded enzymically active derivative from hen egg lysozyme
A S Acharya, H Taniuchi
The Journal of Biological Chemistry
|
November 25, 1976
A study of renaturation of reduced hen egg white lysozyme. Enzymically active intermediates formed during oxidation of the reduced protein
A S Acharya, H Taniuchi
Page
of 9