The Combination of Enzyme and Substrate

نویسنده

  • John H. Northrop
چکیده

1. A quantitative method for the determination of pepsin is described depending on the change in conductivity of a digesting egg albumin solution. 2. The combination of pepsin with an insoluble substrate has been followed by this method. 3. The amount of pepsin removed from solution by a given weight of substrate is independent of the size of the particles of the substrate. 4. There is an optimum zone of hydrogen ion concentration for the combination of enzyme and substrate corresponding to the optimum for digestion. 5. It is suggested that the pepsin combines largely or entirely with the ionized protein.

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

THE PRODUCTION OF GLUCOAMYLASE BY ASPERGILLUS NIGER UNDER SOLID STATE CONDITIONS (RESEARCH NOTE)

In this study, Glucoamylase production by Aspergillus Niger was investigated under solid state conditions with low cost by-products of agricultural processes as substrate. Highest enzyme production was observed when a combination of wheat bran (WB) and corn flour (CF) was used as compared to WB+ rice bran, WB+ rice flour and WB alone. Different additions of (CF) were tested and WB+ 10% CF showe...

متن کامل

Batch Kinetics and Modeling of Alkaline Protease Production by Isolated Bacillus sp. (RESEARCH NOTE)

The aim of this study was the use of fish waste hydrolysate (FWH) as a substrate for alkaline protease production using isolated Bacillus sp. in a batch system. Then the fermentation kinetics of enzyme production was studied. The results show that with the addition of FWH to the fermentation medium with a final concentration of 4% (optimal concentration), alkaline protease value reached a maxim...

متن کامل

The Role of Highly Conserved Tryptophan in the Sixth Conserved Region at Substrate Specificity of α- amylase

Early in this study, an α-Amylase from Bacillus megaterium WHO (BMW) was isolated from hot springs of Ramsar (North of Iran), and its gene was cloned in E.coli. Based on its conserved sequence regions and substrate specificity, it was classified as intermediary group enzymes with the specificity of oligo-1,6-glucosidase and neopullulanase subfamilies. In the sixth conserved re...

متن کامل

Enzyme Immobilization: The State of Art in Biotechnology

The advantages of immobilized enzyme over its soluble counterpart arise from their improved stability andeasy separation from the reaction media, leading to decrease in production cost. Immobilization methodsrange from adsorption onto matrices, entrapment, cross-linking and covalent bonding to prefabricatedcarriers or activated supports. Changes in kinetic properties of immobi...

متن کامل

The Relationship between Cation-Induced Substrate Configuration and Enzymatic Activity of Phosphatidate Phosphohydrolase from Human Liver

The mechanism by which bi-and trivalent cations affect human liver phosphatidatephosphohydrolase (PAP) activity was investigated. Bivalent cations up to 1 mM increased PAP activity whereas at higher concentrations the activity of the enzyme decreased. The stimulatory concentration for trivalent cations such as Al3+ and Cr3+, however, was much lower being 2 m M and 1 m M, respectively. All catio...

متن کامل

Analytical Solution of Steady State Substrate Concentration of an Immobilized Enzyme Kinetics by Laplace Transform Homotopy Perturbation Method

The nonlinear dynamical system modeling the immobilized enzyme kinetics with Michaelis-Menten mechanism for an irreversible reaction without external mass transfer resistance is considered. Laplace transform homotopy perturbation method is used to obtain the approximate solution of the governing nonlinear differential equation, which consists in determining the series solution convergent to the...

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:
  • The Journal of General Physiology

دوره 2  شماره 

صفحات  -

تاریخ انتشار 2003