SPECIFIC DEGRADATION OF CRYPTOCOCCUS NEOFORMANS 3723 CAPSULAR POLYSACCHARIDE BY A MICROBIAL ENZYME: I. ISOLATION, PARTIAL PURIFICATION, AND PROPERTIES OF THE ENZYME

1961 ◽  
Vol 7 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Hans H. Gadebusch ◽  
John D. Johnson

A partially purified intracellular enzyme from a species of Alcaligenes is described which specifically initiates the degradation of the he heteropolysaccharide of Cryptococcus neoformans, isolate 3723, The enzyme is active in the presence of serum and can be inactivated by heating at 45 °C for 10 minutes, The kinetics of the enzyme reaction are similar to those of other enzymes. Recovery and identification of the four known monosaccharides from enzymatic hydrolyzates suggest the presence of a number of other enzymes in these preparations.

2005 ◽  
Vol 73 (12) ◽  
pp. 8429-8432 ◽  
Author(s):  
Lauren E. Yauch ◽  
Michael K. Mansour ◽  
Stuart M. Levitz

ABSTRACT Cryptococcus neoformans capsular glucuronoxylomannan (GXM) is shed during cryptococcosis and taken up by macrophages. The roles of the putative GXM receptors CD14, CD18, Toll-like receptor 2 (TLR2), and TLR4 in GXM clearance from serum and deposition in the liver and spleen in receptor-deficient mice were studied. While alterations in the kinetics of GXM redistribution were seen in the mutant mice, none of the receptors was absolutely required for serum clearance or hepatosplenic accumulation.


1972 ◽  
Vol 18 (12) ◽  
pp. 1953-1957 ◽  
Author(s):  
F. S. Liu ◽  
J. E. Zajic

The intracellular enzyme, L-asparaginase, from aerobically grown Erwinia aroideae NRRL B-138 has been purified and some of its properties studied. Sonic treatment permitted recovery of 95% of L-asparaginase from cells. The crude cell lysate was purified 167-fold by means of ammonium sulfate fractionation and column chromatography on hydroxylapatite–cellulose, and DEAE–Sephadex. The specific activity of the most active fraction of L-asparaginase is 256 IU/mg protein. The enzyme has a broad pH activity profile with maximum at pH 9.0–9.5. The optimum temperature for enzyme reaction was determined to be 41 °C. The apparent activation energy is 11 000 cal/mole. The molecular weight of L-asparaginase was estimated by gel filtration to be 108 000.


1991 ◽  
Vol 81 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Cesar V. Mujer ◽  
Dale W. Kretchman ◽  
A. Raymond Miller

1995 ◽  
Vol 94 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Mohamed Benichou ◽  
Gracia Martinez-Reina ◽  
Felix Romojaro ◽  
Jean-Claude Pech ◽  
Alain Latche

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