S. Latt

Thermolysin: a zinc metalloenzyme.

B. Vallee, B. Holmquist, S. Latt, 1969, Biochemical and biophysical research communications.

Protein-nucleic acid interactions. II. Oligopeptide-polyribonucleotide binding studies.

H. A. Sober, S. Latt, 1967, Biochemistry.

Cobalt Proteases: Implications of Absorption and Circular Dichroism Spectra for Catalysis

B. Vallee, S. Latt, B. Vallée, 1970 .

Protein-nucleic acid interactions. 3. Cation effect on binding strength and specificity.

H. A. Sober, S. Latt, 1967, Biochemistry.

Distance measurements at the active site of carboxypeptidase A during catalysis.

B. Vallee, D. Auld, S. Latt, 1972, Biochemistry.

An approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transfer.

B. Vallee, D. Auld, S. Latt, 1972, Biochemistry.

ENERGY TRANSFER. A SYSTEM WITH RELATIVELY FIXED DONOR-ACCEPTOR SEPARATION.

E. Blout, H. Cheung, S. Latt, 1965, Journal of the American Chemical Society.

Surveyor substrates: energy-transfer gauges of active center topography during catalysis.

D. Auld, B. Valee, S. Latt, 1970, Proceedings of the National Academy of Sciences of the United States of America.

Fluorescende determination of carboxypeptidase A activity based on electronic energy transfer.

B. Vallee, D. Auld, S. Latt, 1972, Analytical biochemistry.