State and reactivity of tryptophyl residues in two bacterial proteases from Sorangium sp.
- 1 June 1975
- journal article
- other
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 393 (2) , 563-570
- https://doi.org/10.1016/0005-2795(75)90083-5
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Content of ATP and ADP in Rabbit BlastocystsNature, 1971
- Primary Structure of α-Lytic Protease: a Bacterial Homologue of the Pancreatic Serine ProteasesNature, 1970
- Reaction of N-bromosuccinimide with lysozymeBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- AMINO ACID AND METAL COMPOSITION OF THE α- AND β-LYTIC PROTEASES OF SORANGIUM SP.Canadian Journal of Biochemistry, 1967
- LYTIC ENZYMES OF SORANGIUM SP.: ISOLATION AND ENZYMATIC PROPERTIES OF THE α- AND β-LYTIC PROTEASESCanadian Journal of Biochemistry, 1965
- LYTIC ENZYMES OF SORANGIUM SP.: A COMPARISON OF THE PROTEOLYTIC PROPERTIES OF THE α- AND β-LYTIC PROTEASESCanadian Journal of Biochemistry, 1965
- LYTIC ENZYMES OF SORANGIUM SP.: A COMPARISON OF SOME PHYSICAL PROPERTIES OF THE α- AND β-LYTIC PROTEASESCanadian Journal of Biochemistry, 1965
- Location of Chromophoric Residues in Proteins by Solvent PerturbationJournal of Biological Chemistry, 1962
- Studies on Adenosine Triphosphate TransphosphorylasesPublished by Elsevier ,1962
- CCCXLII.—Acetylation in aqueous alkaline solutionsJournal of the Chemical Society, 1931