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Literature summary for 4.6.1.18 extracted from

  • Amiri, R.; Bordbar, A.K.; Laurents, D.V.; Khosropour, A.R.; Mohammadpoor-Baltork, I.
    Thermal stability and enzymatic activity of RNase A in the presence of cationic gemini surfactants (2012), Int. J. Biol. Macromol., 50, 1151-1157.
    View publication on PubMed
Search for more literature for 4.6.1.18

Activating Compound

Activating Compound Comment Organism Structure
alkanediyl-alpha,omega-bis(hydroxyethyl methyl hexadecyl ammonium bromide) the cationic gemini surfactants slightly activate and stabilize RNase A below their critical micelle concentrations at pH 5.0. The cationic gemini surfactant with the shorter spacer interacts more efficiently with RNase A than those with longer spacers, two-transition model, UV, circular dichorism and fluorescence spectroscopies, overview Bos taurus
butanediyl-1,4-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
 Bos taurus
hexanediyl-1,6-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
 Bos taurus
pentanediyl-1,5-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bos taurus
-

Synonyms

Synonyms Comment Organism
pancreatic ribonuclease A
-
 Bos taurus
RNase A
-
 Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
 thermal denaturation of RNase A, alone or in the presence of cationic gemini surfactants, is reversible Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Bos taurus