Inhibition of trypsins and chymotrypsins from different animal species: a comparative study.

نویسندگان

  • A Rascón
  • D S Seidl
  • W G Jaffé
  • A Aizman
چکیده

The effect of 3 purified trypsin inhibitors and 4 legume seed extracts on teh trypsins and chymotrypsins of the activated pancreata of 11 animal species, including man, was measured. The activation was performed by either homologous enterokinase or by bovine trypsin. Several trypsinogens were not activated by the latter. Rabbit trypsin was the most sensitive to all inhibitor preparations, while the human trypsin was the most resistant, except to the black bean extract. The response of the chymotrypsins was more variable and those of capybara and rabbit showed extreme sensitivity. Considerable differences between the extracts of black and white garden beans, both Phaseolus vulgaris, with respect to their reactivity toward different animal enzymes were detected. No relation between relative pancreas weight and susceptibility toward soybean trypsin inhibitor could be observed.

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

Characterization of cDNAs Encoding Serine Proteases and Their Transcriptional Responses to Cry1Ab Protoxin in the Gut of Ostrinia nubilalis Larvae

Serine proteases, such as trypsin and chymotrypsin, are the primary digestive enzymes in lepidopteran larvae, and are also involved in Bacillus thuringiensis (Bt) protoxin activation and protoxin/toxin degradation. We isolated and sequenced 34 cDNAs putatively encoding trypsins, chymotrypsins and their homologs from the European corn borer (Ostrinia nubilalis) larval gut. Our analyses of the cD...

متن کامل

Finding protein-protein interaction patterns by contact map matching.

We propose a novel method for defining patterns of contacts present in protein-protein complexes. A new use of the traditional contact maps (more frequently used for representation of the intra-chain contacts) is presented for analysis of inter-chain contacts. Using an algorithm based on image processing techniques, we can compare protein-protein interaction maps and also obtain a dissimilarity...

متن کامل

Digestive proteinases of Artemesia longinaris (Decapoda, Penaeidae) and relationship with molting.

Digestive proteinase activities of Artemesia longinaris were assayed at different stages of the molting cycle. Total proteolytic activity in the hepatopancreas was highest during postmolt. Trypsin and chymotrypsin activities were highest during intermolt. Specific inhibitors and zymograms of A. longinaris hepatopancreas extracts showed four trypsins (14.79, 15.49, 16.60, 17.38 kDa, respectively...

متن کامل

Comparative studies on calpain activity of different muscles of cattle, camel, sheep and goat

Tenderness is the single most important factor influencing consumer acceptance of meat. The calpain proteolytic system is known to be responsible for the post-mortem tenderization of meat. The purpose of this study was to determine and compare the tensile strength and total calpain activities in different muscles of camel, cattle, sheep and goat. In camels, the effect of age and sex of animal w...

متن کامل

IDENTIFICATION OF LEISHMANIA SPECIES FROM DIFFERENT PARTS OF IRAN USING A RANDOM AMPLIFIED POLYMORPHIC DNA IN HUMANS, ANIMAL RESERVOIRS AND VECTORS

In this study, we used Random Amplified Polymorphic DNA (RAPD) for identification of 17 isolates of Leishmania from the skin and reticuloendothelial system of humans, animal reservoirs (rodent and dog) and sandflies in various parts of Iran in the last decade. Fifteen species have been confirmed by isoenzyme characterization by the London School of Hygiene and Tropical Medicine and Shiraz ...

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:
  • Comparative biochemistry and physiology. B, Comparative biochemistry

دوره 82 2  شماره 

صفحات  -

تاریخ انتشار 1985