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86094067

Beta-Amylases from Alfalfa (Medicago sativa L.) Roots.

Beta-Amylases from Alfalfa (Medicago sativa L.) Roots.



 

         
  No.  Divisions/Titles for Abstract Details

 
  1 Abstract Title Beta-Amylases from Alfalfa (Medicago sativa L.) Roots.  
  2 Abstract Source Plant Physiology, 69, 1096-1102.  
  3 Abstract Author(s) Doehlert, D. C., Duke, S. H. & Anderson, L.   
  4 Article Affiliation Department ofAgronomy (D. C. D., S. H. D.) and Department of Biochemistry (L. A.) University of Wisconsin, Madison, Wisconsin 53706.  
  5 Abstract Amylase (an enzyme that helps digest carbohydrates. It is made in the pancreas and the glands that make saliva. When the pancreas is diseased or inflamed, amylase releases into the blood)was found in high activity (193 international units per milligram protein) in the tap root (a straight tapering root growing vertically downwards and forming the centre from which subsidiary rootlets spring.)of alfalfa (Medicago sativa L. cv. Sonora). The activity was separated by gel filtration chromatography (Gel filtration (GF) chromatography separates proteins solely on the basis of molecular size. Separation is achieved using a porous matrix to which the molecules, for steric reasons, have different degrees of access--i.e., smaller molecules have greater access and larger molecules are excluded from the matrix)into two fractions with molecular weights of 65,700 (heavy amylase) and 41,700 (light amylase). Activity staining of electrophoretic gels (Gel electrophoresis is a laboratory method used to separate mixtures of DNA, RNA, or proteins according to molecular size. In gel electrophoresis, the molecules to be separated are pushed by an electrical field through a gel that contains small pores.)indicated the presence of one isozyme in the heavy amylase fraction and two in the light amylase fraction. Three amylase isozymes with electrophoretic mobilities identical to those in the heavy and the light amylase fractions were the only amylases identified in crude root preparations. Both heavy and light amylases hydrolyzed amylopectin, soluble starch, and amylose but did not hydrolyze pullulan or β-limit dextrin. The ratio of viscosity change to reducing power production during starch hydrolysis was identical for both alfalfa amylase fractions and sweet potato β-amylase, while that of bacterial α-amylase was considerably higher. The identification of maltose and β-limit dextrin (Dextrins are a group of low-molecular-weight carbohydrates produced by the hydrolysis of starch or glycogen)as hydrolytic end-products confirmed that these alfalfa root amylases are all β-amylases.
 
  6 Summary The identification of maltose and β-limit dextrin as hydrolytic end-products confirmed that these alfalfa root amylases are all β-amylases.  
  7 Article Published Date 1982  
  8
Study Type invitro  
  9
Substances alfalfa  
  10
Diseases complostion study for enzymes  
  11 Pharmacological Actions Amylase enzyme  
  12
Link https://goo.gl/jeZW6H  
       

 


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