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Hemolytic activity in the periodontopathogen Porphyromonas gingivalis: kinetics of enzyme release and localization.
Chu L, Bramanti TE, Ebersole JL, Holt SC. Chu L, et al. Infect Immun. 1991 Jun;59(6):1932-40. doi: 10.1128/IAI.59.6.1932-1940.1991. Infect Immun. 1991. PMID: 2037355 Free PMC article.
Hemolytic activity was inhibited by proteinase K, trypsin, the proteinase inhibitors Na-P-tosyl-L-lysine chloromethyl ketone and benzamidine, the metabolic inhibitor M-chlorophenyl-hydrazone, and iodoacetate. ...
Hemolytic activity was inhibited by proteinase K, trypsin, the proteinase inhibitors Na-P-tosyl-L-lysine chloromethyl ketone and benz …
Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities.
Chu L, Ebersole JL, Kurzban GP, Holt SC. Chu L, et al. Infect Immun. 1997 Aug;65(8):3231-8. doi: 10.1128/IAI.65.8.3231-3238.1997. Infect Immun. 1997. PMID: 9234780 Free PMC article.
Cystathionine and S-aminoethyl-L-cysteine were also substrates for the protein. Gas chromatography-mass spectrometry and high-performance liquid chromatography analysis of the end products revealed NH3, pyruvate, homocysteine (from cystathionine), and cysteamine (from S-am …
Cystathionine and S-aminoethyl-L-cysteine were also substrates for the protein. Gas chromatography-mass spectrometry and high-perform …
Cystalysin, a 46-kDa L-cysteine desulfhydrase from Treponema denticola: biochemical and biophysical characterization.
Chu L, Ebersole JL, Kurzban GP, Holt SC. Chu L, et al. Clin Infect Dis. 1999 Mar;28(3):442-50. doi: 10.1086/515164. Clin Infect Dis. 1999. PMID: 10194060
With L-cysteine as substrate, cystalysin obeys Michaelis-Menten kinetics. Cystathionine and s-aminoethyl-L-cysteine were also substrates. ...The enzymatic activity was increased by beta-mercaptoethanol and was not inhibited by the proteinase inhibitor TLCK (N alpha- …
With L-cysteine as substrate, cystalysin obeys Michaelis-Menten kinetics. Cystathionine and s-aminoethyl-L-cysteine were also …
Sulfhemoglobin formation in human erythrocytes by cystalysin, an L-cysteine desulfhydrase from Treponema denticola.
Kurzban GP, Chu L, Ebersole JL, Holt SC. Kurzban GP, et al. Oral Microbiol Immunol. 1999 Jun;14(3):153-64. doi: 10.1034/j.1399-302x.1999.140303.x. Oral Microbiol Immunol. 1999. PMID: 10495709
The enzyme was not functional as an L-alanine transaminase, and had a strong preference for L-cysteine over D-cysteine. Cystalysin preferred small alpha-L-amino acids as substrates or inhibitors and was far more active towards L-cysteine than towards t …
The enzyme was not functional as an L-alanine transaminase, and had a strong preference for L-cysteine over D-cysteine. Cystal …
Hemoxidation and binding of the 46-kDa cystalysin of Treponema denticola leads to a cysteine-dependent hemolysis of human erythrocytes.
Chu L, Ebersole JL, Holt SC. Chu L, et al. Oral Microbiol Immunol. 1999 Oct;14(5):293-303. doi: 10.1034/j.1399-302x.1999.140505.x. Oral Microbiol Immunol. 1999. PMID: 10551156
Substrates for the enzyme (including L-cysteine and beta-chloroalanine) enhanced the interaction, which occurred with both whole red blood cells as well as with isolated and purified red blood cell ghosts. ...
Substrates for the enzyme (including L-cysteine and beta-chloroalanine) enhanced the interaction, which occurred with both whole red …
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