-transparent.png){kind=logo}
Hyaluronidase from rhesus monkey testes was purified by detergent extraction, ammonium sulphate fractionation, Sephadex G-200 column chromatography and concanavalin A-Sepharose affinity chromatography. The purified hyaluronidase showed one protein band on acrylamide gel electrophoresis. Antibodies to the purified hyaluronidase were raised in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. The enzyme had a molecular weight of 62,000. The Km was 0.5 mg/ml for hydrolysis of hyaluronic acid at 37 degrees C. The optimum pH for the enzyme was 5.0 but activity was present over a broad pH range. The hyaluronidase was inhibited by HgCl2, CuSO4, FeSO4 and p-chloromercuribenzoate all at a concentration of 2 x 10(-4) M. Cysteine protected the enzyme against HgCl2 inhibition.
M R Bansal, and
K C Kanwar, and
G S Gupta
September 1976,
Journal of reproduction and fertility,
M R Bansal, and
K C Kanwar, and
G S Gupta
January 1975,
Journal of medical primatology,
M R Bansal, and
K C Kanwar, and
G S Gupta
February 1977,
Infection and immunity,
M R Bansal, and
K C Kanwar, and
G S Gupta
February 1970,
The British veterinary journal,
M R Bansal, and
K C Kanwar, and
G S Gupta
July 2008,
Animal cognition,
M R Bansal, and
K C Kanwar, and
G S Gupta
February 1974,
Fertility and sterility,
M R Bansal, and
K C Kanwar, and
G S Gupta
May 2011,
Animal cognition,
M R Bansal, and
K C Kanwar, and
G S Gupta
January 1969,
Folia primatologica; international journal of primatology,
M R Bansal, and
K C Kanwar, and
G S Gupta
January 1984,
Veterinary pathology,
M R Bansal, and
K C Kanwar, and
G S Gupta
July 1994,
Journal of medical primatology,
