Isolation of human renin inhibitor from soybean: soyasaponin I is the novel human renin inhibitor in soybean.

نویسندگان

  • Saori Takahashi
  • Kazuyuki Hori
  • Mamoru Shinbo
  • Kazuyuki Hiwatashi
  • Takeshi Gotoh
  • Seihan Yamada
چکیده

We found human renin inhibitory activity in soybean and isolated the active compound, soybean renin inhibitor (SRI). The physico-chemical data on the isolated SRI were identical with those of soyasaponin I. SRI showed significant inhibition against recombinant human renin, with an IC(50) value of 30 microg/ml. Kinetic studies with SRI indicated partial noncompetitive inhibition, with a K(i) value of 37.5 microM. On the other hand, SRI weakly inhibited pepsin, papain, and bromeline activities, but did not inhibit other proteinases, such as trypsin, kallikrein, angiotensin converting enzyme, and aminopeptidase M. Moreover, a significant (p<0.05) decrease in the systolic blood pressure of spontaneously hypertensive rats was observed when partially purified SRI was orally administrated at 40 mg/kg/d for 7 weeks. This is the first demonstration of a renin inhibitor from soybean, soyasaponin I.

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

Predictive Modeling of Phenylpiperazine Derivatives for Renin Inhibition.

The renin–angiotensin–aldosterone system is the well established endocrine system having significant role in preserving hemodynamic stability. Renin is secreted from the juxtaglomerular cells of the kidney. Phenylpiperazine derivatives have been reported as human renin inhibitor. To perform predictive QSAR modeling for 27 phenylpiperazine derivatives as renin enzyme inhibitors. The IC50 values ...

متن کامل

Refolding and activation of human prorenin expressed in Escherichia coli: application of recombinant human renin for inhibitor screening.

Human prorenin was expressed in Escherichia coli as a fusion protein of thioredoxin. The chimeric protein, which accumulated insoluble inclusion bodies, was solubilized in 4 M guanidine-HCl and refolded by an arginine-detergent buffer system and by systematic dialysis. The refolded fusion prorenin was activated by trypsin. The antiserum against human kidney renin specifically inhibited the reco...

متن کامل

Renin Inhibitors in Foodstuffs: Structure-Function Relationship

Renin, a highly specific aspartic proteinase originated from kidney, is a ratelimiting enzyme in renin-angiotensin system. Recently, we developed effective expression system for recombinant human (rh) renin using baculovirus-insect cell expression system, and simple and rapid assay method for rh-renin using internally quenched fluorogenic (IQF) substrate. Using the purified rh-renin and the IQF...

متن کامل

Cyclothiazomycin, a novel polythiazole-containing peptide with renin inhibitory activity. Taxonomy, fermentation, isolation and physico-chemical characterization.

Cyclothiazomycin is a novel renin inhibitor produced by Streptomyces sp. NR0516. It was isolated from fermentation broth by extraction with butyl alcohol, QAE-Toyopearl column chromatography and preparative HPLC. Cyclothiazomycin, which was determined to be a unique polythiazole-containing bicyclic peptide, exhibited inhibitory activity against human plasma renin with IC50 being 1.7 microM.

متن کامل

Isolation and Characterization of Trypsin Inhibitors (Kunitz Soybean Trypsin Inhibitor, Bowman-birk Inhibitor) in Soybean

Soybean (Glycine max (L.) Merr.) has emerged as one of the most economical and nutritious foods. Kunitz Soybean Trypsin Inhibitor (KSTI) and Bowman -Birk Inhibitor (BBI) are the two major trypsin inhibitors in soybeans. The ingested soybean trypsin inhibitors cause growth depression as demonstrated in different animal species and human. The main part of the present study was devoted to isolatio...

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:
  • Bioscience, biotechnology, and biochemistry

دوره 72 12  شماره 

صفحات  -

تاریخ انتشار 2008