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Kinetics of trypsin inhibition by its specific inhibitors

Biochemistry (Easton), 1989-02, Vol.28 (3), p.1070-1076

1989

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Association and dissociation of protein disulfide isomerase

Biochimica et biophysica acta, 1994-07, Vol.1207 (1), p.109-113

1994

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Dissociation and aggregation of d-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride

Biochimica et biophysica acta, 1990-04, Vol.1038 (2), p.240-246

1990

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Resynthesis of insulin from its A and B chains in the presence of denaturants

Biochemical and biophysical research communications, 1987-07, Vol.146 (2), p.437-442

1987

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Kinetics of inactivation of creatine kinase during modification of its thiol groups

Biochemistry (Easton), 1988-07, Vol.27 (14), p.5095-5100

1988

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FTIR studies of secondary structures of bovine insulin and its derivatives

Biochimica et biophysica acta, 1991-10, Vol.1080 (1), p.29-33

1991

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Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase

Biochimica et biophysica acta, 1986-01, Vol.869 (1), p.69-74

1986

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Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds

The Journal of biological chemistry, 1994-10, Vol.269 (40), p.24550-24552

1994

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High concentrations of d-glyceraldehyde-3-phosphate dehydrogenase stabilize the enzyme against denaturation by low concentrations of GuHCl

Biochimica et biophysica acta, 2000-09, Vol.1481 (2), p.283-288

2000

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Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride

Biochimica et biophysica acta, 1996-07, Vol.1295 (2), p.239-244

1996

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Reactivation Kineties of diethylphosphoryl acetylcholine esterase

European journal of biochemistry, 1985-09, Vol.151 (3), p.525-529

1985

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Comparison of inactivation and conformational changes of d-glyceraldehyde-3-phosphate dehydrogenase during thermal denaturation

Biochimica et biophysica acta, 1990-04, Vol.1038 (2), p.247-252

1990

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The presence of reactive SH groups in the enzymatically active dicyano derivative of creatine kinase

Biochimica et biophysica acta, 1987-01, Vol.911 (2), p.136-143

1987

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Conformational and activity changes during guanidine denaturation of d-glyceraldehyde-3-phosphate dehydrogenase

Biochimica et biophysica acta, 1987-01, Vol.911 (1), p.19-24

1987

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Is the subunit the minimal function unit of creatine kinase?

Biochimica et biophysica acta, 1990-07, Vol.1039 (3), p.313-317

1990

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Number of ways of joining SH groups to form multi-peptide chain proteins

Journal of theoretical biology, 1987-02, Vol.124 (3), p.293-301

1987

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The inactivation kinetics of papain by guanidine hydrochloride: a re-analysis

Biochimica et biophysica acta, 1998-10, Vol.1388 (1), p.84-92

1998

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Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation

Biochimica et biophysica acta, 1989-07, Vol.997 (1), p.78-82

1989

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Activation of chicken liver dihydrofolate reductase in concentrated urea solutions

Biochimica et biophysica acta, 1995-09, Vol.1252 (1), p.151-157

1995

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An essential tryptophan residue for rabbit muscle creatine kinase

Biochimica et biophysica acta, 1985-07, Vol.830 (1), p.59-63

1985

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Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation

Biochemistry (Easton), 1984-06, Vol.23 (12), p.2740-2744

1984

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Protein disulfide isomerase is both an enzyme and a chaperone

The FASEB journal, 1993-12, Vol.7 (15), p.1515-1517

1993

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Comparison of secondary structures of insulin and proinsulin by FTIR

Journal of protein chemistry, 1993-08, Vol.12 (4), p.483-487

1993

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Inactivation kinetics of the reduced spinach chloroplast fructose-1,6-bisphosphatase by subtilisin

European journal of biochemistry, 1997-09, Vol.248 (3), p.925-929

1997

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The role of active site flexibility in enzyme catalysis

Biochemistry (Moscow), 1998-03, Vol.63 (3), p.253-258

Tsou, C L

1998

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Kinetics of trypsin inhibition by its specific inhibitors

Association and dissociation of protein disulfide isomerase

Dissociation and aggregation of d-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride

Resynthesis of insulin from its A and B chains in the presence of denaturants

Kinetics of inactivation of creatine kinase during modification of its thiol groups

FTIR studies of secondary structures of bovine insulin and its derivatives

Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase

Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds

High concentrations of d-glyceraldehyde-3-phosphate dehydrogenase stabilize the enzyme against denaturation by low concentrations of GuHCl

Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride

Reactivation Kineties of diethylphosphoryl acetylcholine esterase

Comparison of inactivation and conformational changes of d-glyceraldehyde-3-phosphate dehydrogenase during thermal denaturation

The presence of reactive SH groups in the enzymatically active dicyano derivative of creatine kinase

Conformational and activity changes during guanidine denaturation of d-glyceraldehyde-3-phosphate dehydrogenase

Is the subunit the minimal function unit of creatine kinase?

Number of ways of joining SH groups to form multi-peptide chain proteins

The inactivation kinetics of papain by guanidine hydrochloride: a re-analysis

Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation

Activation of chicken liver dihydrofolate reductase in concentrated urea solutions

An essential tryptophan residue for rabbit muscle creatine kinase

Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation

Protein disulfide isomerase is both an enzyme and a chaperone

Comparison of secondary structures of insulin and proinsulin by FTIR

Inactivation kinetics of the reduced spinach chloroplast fructose-1,6-bisphosphatase by subtilisin

The role of active site flexibility in enzyme catalysis

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