Purificationand Properties of Aminopeptidase C Chicken Sketetal Muscle from

نویسندگان

  • Toshihide NisHiMuRA
  • Yutaka KATo
چکیده

Aminopeptidase C was purified from fresh chicken skeletal muscle by arnmonium sulfate fract;onation,andbysuccessivechromatographyonDEAE-cellulose,UltrogelAcA34,DEAE-cellulose again, and an alanine AH-Sepharose 4B ftMnity column twice. The purificd enzyme migrated as a s;ngle band by SDS-PAGE. Am;nopeptidase C was purified about 300-fo1cl over the crllde extraet with a },ield of O.6%. The molecular weight of this enzyme was found to be 18S,OOO by get filtration in a Sepharose 6B colllmn a"d 9Z,OOO by SDS-PAGE. The optimum pH for thc hydrolysis of L,-lellcine fi-naphthylamide wfts 6.0-7.e, the enzyme being stab[e in the range of pH 6.5-8.0. The aetivity of this enzyme was strongly inhibited by, EDTA and p"romycin, and was high against the fi-naphthylamide deriyatiyes of I.ys, Lell, Ala and Met. The enzyme was mere actiye towards triand tetrapeptides than towards dipeptides.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Effects of concanavalin A on intestinal brush border enzyme activity in broiler chickens.

1. The effects of Concanavalin A (Con A) on enzymes from the intestinal brush border were studied using membrane vesicles (BBMV) prepared from 3- and 6-week-old broiler chickens. 2. Maltase, sucrase, phytase, alkaline phosphatase and leucine aminopeptidase activities were assayed in BBMV in the absence (T0) or presence (T1) of Con A, or in the presence of casein (T2). Disaccharidase specific ac...

متن کامل

Chicken intestinal aminopeptidase: partial sequence of the gene, expression and activity.

Aminopeptidases are members of a membrane-bound metallopeptidase family that are expressed at a high level on the brush-border membrane of enterocytes. Because the rapid growth of meat-type chickens depends on the dietary supply of amino acids, a study of intestinal aminopeptidases, which play a central role in protein digestion, is important. This study is the first reported isolation of the p...

متن کامل

Digestive alkaline proteases from the Tunisian barbell (Barbus callensis): Characterization and application as a detergent additive, in chicken feather-degradation and as a dehairing agent

Alkaline crude enzymes from the viscera of the Tunisian barbel (Barbus callensis) were extracted and characterized. Proteolytic crude extract from barbel viscera was active and stable in alkaline solution. The optimum pH and temperature were 11.0 and 55 °C, respectively, using casein as a substrate. The crude alkaline protease was extremely stable in the pH range of 5.0-12.0. Zymography activit...

متن کامل

Digestive alkaline proteases from the Tunisian barbell (Barbus callensis): Characterization and application as a detergent additive, in chicken feather-degradation and as a dehairing agent

Alkaline crude enzymes from the viscera of the Tunisian barbel (Barbus callensis) were extracted and characterized. Proteolytic crude extract from barbel viscera was active and stable in alkaline solution. The optimum pH and temperature were 11.0 and 55 °C, respectively, using casein as a substrate. The crude alkaline protease was extremely stable in the pH range of 5.0-12.0. Zymography activit...

متن کامل

The effect of obidoxime on reversal or prevention of paraoxon-induced changes in the function of Chicken biventer cervices nerve-muscle preparation

Paralysis of skeletal muscles, which can lead to paralysis of respiratory muscles and death, is one of the most toxic effects of organophosphates (OPs), and oximes are the only available antidotes that can reverse or prevent such toxic effects. In the present study, the possible reversal or preventive effect of different concentrations of obidoxime (toxogonin) on changes induced by paraoxon (as...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2018