The changes of circular dichroism and fluorescence spectra, and the comparison with inactivation rates of angiotensin converting enzyme in guanidine solutions
- 30 April 1990
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1039 (1) , 61-66
- https://doi.org/10.1016/0167-4838(90)90226-6
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Activity change during unfolding of bovine pancreatic ribonuclease A in guanidineBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplicationAnalytical Biochemistry, 1986
- The functional role of zinc in angiotensin converting enzyme: implications for the enzyme mechanismJournal of Inorganic Biochemistry, 1985
- Inhibition of angiotensin converting enzyme: mechanism and substrate dependenceBiochemistry, 1984
- Affinity chromatographic purification of angiotensin converting enzymeBiochemistry, 1984
- Activation of angiotensin converting enzyme by monovalent anionsBiochemistry, 1983
- Substrate specificity and kinetic characteristics of angiotensin converting enzymeBiochemistry, 1983
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951