Normal view MARC view ISBD view

Xanthine oxidase associated with the milk fat globule membrane of buffalo's milk [electronic resource]: isolation, and physicochemical properties.

By:

Ismail, Azza

Contributor(s):

Language: English Summary language: Arabic Description: P.1403-1419Other title:

إنزيم الزانثين أوكسيديز المصاحب لغشاء حبيبة الدهن فى اللبن الجاموسي: عزله وتنقيته وخواصه الفيزوكيميائية [Added title page title]

Uniform titles:

Minufiya journal of agricultural research, 2003 V. 28 (5) Part one [electronic resource].

Subject(s):

Online resources:

Full Text Article.

In: Minufiya Journal of Agricultural Research 2003.v.28(5)P.1Summary: Xanthine Oxidase (XO) was isolated from Buffalo's milk fat globule membrane (MFGM). The enzyme was purified on Sephadex G-100 column (45x2.5cm). One hundred twenty milligrams of a purified XO preparation were yielded from 15 liters of whole Buffalo's milk, representing a 13.69-fold purification. When washed-cream buttermilk was the starting source for the XO, approximately 63% of the indigenous enzyme was yielded in the isolate. The isolated enzyme possessed Michaelis-constant of (Km) of 50 and a maximum initial velocity (Vmax) 1.11 Umoles /mg/min. Molecular weight (MW) estimated by gel filtration methods using a Sephadex G-100 was about 150 KDa. An energy of activation of 15.49 Kcal / mol for the OX activity was derived from the Arrhenius plot of initial velocity (Vo) across a temperature ranging from 15 to 30°C.

Average rating: 0.0 (0 votes)

No physical items for this record

Includes reference.

Xanthine Oxidase (XO) was isolated from Buffalo's milk fat globule membrane (MFGM). The enzyme was purified on Sephadex G-100 column (45x2.5cm). One hundred twenty milligrams of a purified XO preparation were yielded from 15 liters of whole Buffalo's milk, representing a 13.69-fold purification. When washed-cream buttermilk was the starting source for the XO, approximately 63% of the indigenous enzyme was yielded in the isolate. The isolated enzyme possessed Michaelis-constant of (Km) of 50 and a maximum initial velocity (Vmax) 1.11 Umoles /mg/min. Molecular weight (MW) estimated by gel filtration methods using a Sephadex G-100 was about 150 KDa. An energy of activation of 15.49 Kcal / mol for the OX activity was derived from the Arrhenius plot of initial velocity (Vo) across a temperature ranging from 15 to 30°C.

Summary in Arabic.

There are no comments on this title.

to post a comment.