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The Isolation and Kinetics of Lactoperoxidase

B. Burec ; Biochemical Laboratory, Faculty of T ec hnology, University of Zagreb, Zagreb, Croatia, Yugoslavia
M. Jušić ; Biochemical Laboratory, Faculty of T ec hnology, University of Zagreb, Zagreb, Croatia, Yugoslavia
P. Mildner ; Biochemical Laboratory, Faculty of T ec hnology, University of Zagreb, Zagreb, Croatia, Yugoslavia


Puni tekst: engleski pdf 7.204 Kb

str. 153-159

preuzimanja: 90

citiraj


Sažetak

The catalatic and peroxidatic activities of lactoperoxidase
and horse-ra dish peroxidase are described. For measuring the
peroxidatic activity. pyrogallol was used as a hydrogen donor. A
manometric m ethod was used for the determination of the Km
value. The Km value for the catalatic reaction was calculated on
the basis of 0 2 evolved, a nd the peroxidatic reaction was calculated
on the basis of C02 evolved. In the catalatic reaction the
efficiency of lactoperoxidase and horse-radish peroxidase are of
the same order. The peroxidatic activity of lactoperoxidase is
higher than that of horse-radish peroxidase. The mechanism of
peroxidase action was interpreted as described by Chancet.

Ključne riječi

Hrčak ID:

208331

URI

https://hrcak.srce.hr/208331

Posjeta: 229 *