Studies on streptococcal proteinase

1990 ◽  
Vol 18 (4) ◽  
pp. 593-594 ◽  
Author(s):  
HAYLEY FRENCH ◽  
RALPH WILLIAMS ◽  
ERDJAN SALIH ◽  
DEVANAND KOWLESSUR ◽  
KEITH BROCKLEHURST
Keyword(s):  
Streptococcal Proteinase

scholarly journals Chemical Properties of Streptococcal Proteinase and Its Zymogen

1963 ◽  
Vol 238 (1) ◽  
pp. 251-256
Author(s):  
Teh-Yung Liu ◽  
Norbert P. Neumann ◽  
Stuart D. Elliott ◽  
Stanford Moore ◽  
William H. Stein
Keyword(s):  
Chemical Properties ◽  
Streptococcal Proteinase

scholarly journals Streptococcal Proteinase-catalyzed Hydrolysis of Some Ester and Amide Substrates

1969 ◽  
Vol 244 (20) ◽  
pp. 5745-5756
Author(s):  
Teh-Yung Liu ◽  
Noboru Nomura ◽  
Elsy K. Jonsson ◽  
Bruce G. Wallace
Keyword(s):  
Streptococcal Proteinase ◽  
Hydrolysis Of

Synthese einer partialsequenz aus dem aktiven zentrum der streptokokken-protease (ec 3.4.22.10), iv / Synthesis of a fragment of the active center of the streptococcal proteinase, iv

1974 ◽  
Vol 29 (9-10) ◽  
pp. 457-463 ◽  
Author(s):  
Eugen Schaich ◽  
Friedhelm Schneider
Keyword(s):  
Active Center ◽  
Sh Group ◽  
Streptococcal Proteinase

Abstract The synthesis of the protected peptide Boc-His-Cys (M Bzl)-Val-Ala-Thr-Ala-N2H3 (OH) is de­ scribed. This peptide is a fragment of an active center sequence of the streptococcal proteinase (EC 3.4.22.10) containing the essential SH-group of the enzyme

Mechanism of action of streptococcal proteinase. I. Active-site titration

Biochemistry ◽  
1973 ◽  
Vol 12 (2) ◽  
pp. 320-327 ◽  
Author(s):  
A. A. Kortt ◽  
Teh-Yung Liu
Keyword(s):  
Mechanism Of Action ◽  
Active Site ◽  
Streptococcal Proteinase

Activation of Streptococcal Proteinase and its Zymogen by Bacterial Cell Walls

Nature ◽  
1965 ◽  
Vol 206 (4979) ◽  
pp. 33-34 ◽  
Author(s):  
T. Y. LIU ◽  
S. D. ELLIOTT
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Cell Walls ◽  
Streptococcal Proteinase

scholarly journals VARIATION OCCURRING IN GROUP A STREPTOCOCCI DURING HUMAN INFECTION

1948 ◽  
Vol 87 (6) ◽  
pp. 521-533 ◽  
Author(s):  
Sidney Rothbard ◽  
Robert F. Watson
Keyword(s):  
T Antigen ◽  
Human Infection ◽  
M Protein ◽  
Group A Streptococci ◽  
Upper Respiratory Tract ◽  
Group A ◽  
Normal Human ◽  
Streptococcal Proteinase ◽  
Relationship Of ◽  
Observation Period

A study was made of the variation occurring in group A streptococci during the natural course of infection in man. From 54 patients with 56 different group A streptococcal infections of the upper respiratory tract, 251 strains of streptococci, isolated at weekly intervals following infection, were tested for their capacity to resist the bacteriostatic action of normal human blood. In 52 of the infections the streptococci were of recognized serological types and were also tested for variation in their ability to produce the type-specific M protein antigen. Strains isolated in the 1st week of infection were uniformly highly resistant to bacteriostasis and elaborated large amounts of M substance. In 42 per cent of the 52 infections, strains isolated in the convalescent and carrier stages showed an increasing susceptibility to bacteriostasis correlated with a progressive loss of M substance; whereas in the remaining 58 per cent resistance to bacteriostasis and the capacity to produce M protein were maintained throughout the observation period. In 3 different infections, the streptococci became so degraded that no M protein could be demonstrated in acid extracts of these variants. Concomitantly these strains became highly susceptible to bacteriostasis. Spontaneous reversion did not occur, but serial mouse passage reestablished these functions. These degraded variants had the same T antigen as their respective original strains. No evidence was obtained that variation of group A streptococci in resistance to bacteriostasis or in the ability to produce the type-specific M antigen was associated (a) with the appearance of type-specific bacteriostatic antibodies; (b) with any particular serological type of streptococcus; (c) with the production of streptococcal proteinase which digests the M protein; (d) with the therapeutic administration of sulfadiazine; or (e) with the development of complications. The possible relationship of these observations to the problem of the "dangerous carrier" of group A hemolytic streptococci is discussed.

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