Purification and Properties of the TTX-Sensitive Protein from Bovine Brain Soluble Fraction

1987 ◽  
pp. 187-192
1985 ◽  
Vol 33 (4) ◽  
pp. 1334-1341
Author(s):  
KENKICHI TAKAUCHI ◽  
AKIRA TOKUMURA ◽  
JUNICHI YOSHIDA ◽  
TAKEHISA IWAMA ◽  
YASOMI HANDA ◽  
...  

1993 ◽  
pp. 203-207
Author(s):  
Tae Hirakawa-Sakurai ◽  
Kiyoshi Ohkawa ◽  
Makoto Matsuda

1969 ◽  
Vol 112 (3) ◽  
pp. 335-342 ◽  
Author(s):  
A. S. Brecher ◽  
J. B. Suszkiw

1. An enzyme acting on aminoacyl-β-naphthylamides has been isolated from the soluble fraction of bovine brain and purified 205-fold by means of ammonium sulphate fractionation, hydroxyapatite adsorption and DEAE-Sephadex column chromatography. 2. Arylamidase requires thiol groups for retention of its activity, is heat-labile and is susceptible to freezing. p-Chloromercuribenzoate and N-ethylmaleimide inactivate the enzyme rapidly. 3. Metal ions are not required for its activity, but stimulation by Mn2+ and Mg2+ and inactivation by Co2+ and Zn2+ are observed. 4. Optimum pH7·5 in phosphate buffer was exhibited for all substrates tested except l-leucyl-β-naphthylamide, for which optimum pH is 6·5. 5. Km values for a number of substrates have been obtained and substrate inhibition at high concentrations was demonstrated. 6. The molecular weight is approx. 70000 as determined by Sephadex-gel filtration.


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