ph-stat titration allows the continuous determination of ribonuclease A activity toward cytidine 2′,3′-cyclic monophosphate at high substrate concentrations

Analytical Biochemistry

Volumn 305, Issue 2, 2002, Pages 281-284

  Köditz, Jens ^a   Ulbrich Hofmann, Renate ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

CYTIDINE; HIGH SUBSTRATE CONCENTRATIONS; MONOPHOSPHATES; PH-STAT; RIBONUCLEASE A;

CHEMISTRY;

CYCLIC CMP; CYCLIC UMP; CYTIDINE DERIVATIVE; RIBONUCLEASE A; CIFOSTODINE; PANCREATIC RIBONUCLEASE; PYRIMIDINE NUCLEOTIDE;

ARTICLE; CONCENTRATION RESPONSE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME SUBSTRATE; PH MEASUREMENT; PHOSPHATE TRANSPORT; PRIORITY JOURNAL; SPECTROSCOPY; TITRIMETRY; METABOLISM; PH;

CYTOSINE NUCLEOTIDES; HYDROGEN-ION CONCENTRATION; RIBONUCLEASE, PANCREATIC; SPECTRUM ANALYSIS; TITRIMETRY;

EID: 0037096080     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2002.5643     Document Type: Article

References (13)

1. Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate
2. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
3. Alkylation of the methionine residues of ribonuclease in 8 M urea
4. Zum mechanismus der ribonuclease-reaktion. 1. Die aufgabe der pyrimidinbase bei der reaktion
5. m
6. Thermodynamic studies on the hydrolysis of cytidine 2′:3′-phosphate by bovine pancreatic ribonuclease A
7. Some spectrophotometric and polarimetric experiments with ribonuclease
8. Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid
9. Differences in the denaturation behavior of ribonuclease A induced by temperature and guanidine hydrochloride
10. The subsites structure of bovine pancreatic ribonuclease A: Accounts for the abnormal kinetic behavior with cytidine 2′,3′-cyclic phosphate