scholarly journals Studies on lytic enzyme toward cariogenic streptococci. Part VI. Purification and characterization of N-acetylmuramyl-L-alanine amidase from Streptomyces globisporus 1829.

1984 ◽  
Vol 48 (2) ◽  
pp. 261-269 ◽  
Author(s):  
Shigeo KAWATA ◽  
Tadashi TAKEMURA ◽  
Yoshiyuki TAKASE ◽  
Kanae YOKOGAWA
1981 ◽  
Vol 45 (10) ◽  
pp. 2289-2300
Author(s):  
Kiyoshi Hayashi ◽  
Takafumi Kasumi ◽  
Naoya Kubo ◽  
Nobuzo Tsumura

FEBS Letters ◽  
1984 ◽  
Vol 166 (2) ◽  
pp. 293-297 ◽  
Author(s):  
Yoshihiro Matsuda ◽  
Atsuko Yamasaki ◽  
Saito Tatsuaki ◽  
Tetsuya Yamaguchi

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.


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