Study of the Radiometric Method and Use of the Liquid Scintillation Technique for Tool-Wear Determination

1965 ◽  
Vol 87 (1) ◽  
pp. 47-52 ◽  
Author(s):  
G. F. Wilson ◽  
W. Dennis McHenry

A radiometric method of tool-wear evaluation was investigated and evaluated by comparing the results with those obtained from visual wear measurements. A liquid scintillation technique is presented for accurately determining tool wear for cutting limes as low as 0.003 min. It is recommended that the radioactive tracer techniques of measuring tool wear be used as supplemental methods in conjunction with visual wear determination procedures rather than primary methods of evaluating machining variables.

1980 ◽  
Vol 43 (1) ◽  
pp. 167-175
Author(s):  
M.A. Grusak ◽  
R.J. Thomas ◽  
B.H. Marsh

De novo synthesis of wall material by cells of Sphaerocarpos donnellii was followed using radioactive tracer techniques. Uniform uptake of [14C]glucose by plasmolysed suspension cultures was demonstrated autoradiographically. Liquid scintillation counts of acid- or alkali-soluble wall carbohydrates indicate that hemicellulose and cellulose make up the major wall fractions in control and plasmolysed tissues. The amount of label in walls of plasmolysed cells was significantly lower than in those of controls. Higher relative radioactivity in pectin and hemicellulose, and lower radioactivity in cellulose were found in plasmolysed tissue. These compositional changes may enhance wall stability by providing numerous sites for cross-linkage between cellulose microfibrils of regenerated walls.


2003 ◽  
Vol 125 (4) ◽  
pp. 378-384 ◽  
Author(s):  
Stuart Barnes ◽  
Richard Morgan ◽  
Andrew Skeen

Although the abrasive reinforcement in MMCs primarily controls their machining behavior, the properties of the matrix also exert an influence. A 1200 W diode laser was used, due to the large footprint (5×0.3 mm) and the short wavelength (0.94 μm) to pre-treat a 2618 (18% SiC) alloy. The laser heating and self-quenching of the material modified the matrix properties. Machining performance was then assessed by measuring tool wear and edge condition, cutting forces, surface finish, and sub-surface damage. Results indicated that pre-treatment gave less wear, lower forces, and less sub-surface damage although abrasion remained the primary wear mechanism.


2019 ◽  
Author(s):  
Tan Chun Yu ◽  
M. Fathullah ◽  
M. M. A. Abdullah ◽  
Z. Shayfull ◽  
Faheem Tahir
Keyword(s):  
Fly Ash ◽  

1983 ◽  
Vol 157 (4) ◽  
pp. 1239-1251 ◽  
Author(s):  
T Fujita ◽  
N Tamura

Purified C4-binding protein (C4-bp) was shown to bind to cell-bound C4b by radioactive tracer techniques. With EAC4 bearing greater than 3,000 C4b-molecules/cell, the number of C4-bp molecules bound was directly proportional to the number of C4b molecule on the cell surface; EAC4 bearing less than 3,000 C4b-molecules/cell bound a very small amount of C4-bp. Scatchard analysis of binding of C4-bp indicated an equilibrium constant of 4.6 X 10(8) L/M and a maximum of 0.43 C4-bp molecules bound per C4b molecule, equivalent to an average of one molecule of C4-bp per two or three molecules of C4b. Fluid-phase C4b inhibited the binding of C4-bp to cell-bound C4b in a dose-dependent manner, whereas native C4 had little effect. C2 inhibited this binding and also released C4-bp from EAC4,C4-bp. However, C2 was 27 times less effective than unlabeled C4-bp on a molar basis and a considerable amount of C4-bp remained bound to C4b on the cell surface even in the presence of a large excess of C2. We also examined the cofactor activity of C4-bp in the cleavage of cell-bound C4b by C3b/C4b inactivator (I). Cleavage of the alpha' chain of C4b on the cell surface by I alone was incomplete and an intermediate cleavage product, alpha-75, was observed. When C4-bp bound to C4b on the cell surface, the alpha' chain of the C4b cleaved into three fragments, alpha 2, alpha 3, and alpha 4. The alpha 3, alpha 4, beta, and gamma peptides (C4c) were released into the fluid phase, and the alpha 2 fragment (C4d) remained linked covalently to the cell membrane via an ester bond. In some situations, therefore, C4-bp enhances the proteolytic activity of I on cell-bound C4b.


10.2118/654-g ◽  
1956 ◽  
Vol 8 (09) ◽  
pp. 12-17 ◽  
Author(s):  
G.L. Gore ◽  
L.L. Terry

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