scholarly journals Study of Polarographic Anodic Wave in the Presence of Chloride Ions by a New Numerical Method

1988 ◽  
Vol 61 (9) ◽  
pp. 3159-3167 ◽  
Author(s):  
Kenji Kikuchi ◽  
Teisuke Murayama
Keyword(s):  
Numerical Method ◽  
Chloride Ions ◽  
Anodic Wave

Junction of the Epithelium and Lamina Propria of the Bovine Rumen Mucosa

1967 ◽  
Vol 25 ◽  
pp. 68-69
Author(s):  
Al W. Stinson
Keyword(s):  
Osmium Tetroxide ◽  
Squamous Epithelium ◽  
Short Chain Fatty Acids ◽  
Chloride Ions ◽  
Fermentation Products ◽  
Ruminant Species ◽  
Protective Shield ◽  
Stratified Squamous Epithelium ◽  
Lead Hydroxide ◽  
Acetic Acids

The stratified squamous epithelium which lines the ruminal compartment of the bovine stomach performs at least three important functions. (1) The upper keratinized layer forms a protective shield against the rough, fibrous, constantly moving ingesta. (2) It is an organ of absorption since a number of substances are absorbed directly through the epithelium. These include short chain fatty acids, potassium, sodium and chloride ions, water, and many others. (3) The cells of the deeper layers metabolize butyric acid and to a lesser extent propionic and acetic acids which are the fermentation products of rumen digestion. Because of the functional characteristics, this epithelium is important in the digestive process of ruminant species which convert large quantities of rough, fibrous feed into energy.Tissue used in this study was obtained by biopsy through a rumen fistula from clinically healthy, yearling holstein steers. The animals had been fed a typical diet of hay and grain and the ruminal papillae were fully developed. The tissue was immediately immersed in 1% osmium tetroxide buffered to a pH of 7.4 and fixed for 2 hrs. The tissue blocks were embedded in Vestapol-W, sectioned with a Porter-Blum microtome with glass knives and stained with lead hydroxide. The sections were studied with an RCA EMU 3F electron microscope.

Factors Influencing the Separation of Glu-Plasminogen Affinity Forms I and II by Affinity Chromatography

1984 ◽  
Vol 52 (03) ◽  
pp. 347-349 ◽  
Author(s):  
Daan W Traas ◽  
Bep Hoegee-de Nobel ◽  
Willem Nieuwenhuizen
Keyword(s):  
Affinity Chromatography ◽  
Dissociation Constants ◽  
Ionic Composition ◽  
Chloride Ions ◽  
Factors Influencing ◽  
Two Factors ◽  
Human Plasminogen

SummaryNative human plasminogen, the proenzyme of plasmin (E. C. 3.4.21.7) occurs in blood in two well defined forms, affinity forms I and II. In this paper, the feasibility of separating these forms of human native plasminogen by affinity chromatography, is shown to be dependent on two factors: 1) the ionic composition of the buffer containing the displacing agent: buffers of varying contents of sodium, Tris, phosphate and chloride ions were compared, and 2) the type of adsorbent. Two adsorbents were compared: Sepharose-lysine and Sepharose-bisoxirane-lysine. Only in the phosphate containing buffers, irrespective of the type of adsorbent, the affinity forms can be separated. The influence of the adsorbent can be accounted for by a large difference in dissociation constants of the complex between plasminogen and the immobilized lysine.

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