Effects of acid precipitation

1982 ◽  
Vol 16 (3) ◽  
pp. 162-169 ◽  
Author(s):  
Norman R. Glass ◽  
Dean E. Arnold ◽  
James N. Galloway ◽  
George R. Hendrey ◽  
Jeffrey J. Lee ◽  
...  
Keyword(s):  
1964 ◽  
Vol 11 (01) ◽  
pp. 064-074 ◽  
Author(s):  
Robert H Wagner ◽  
William D McLester ◽  
Marion Smith ◽  
K. M Brinkhous

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.


1972 ◽  
Vol 70 (1) ◽  
pp. 48-55 ◽  
Author(s):  
Mario A. Pisarev ◽  
Noe Altschuler ◽  
Leslie J. DeGroot

ABSTRACT The process of secretion of the thyroid hormone involves several steps: pinocytosis of thyroglobulin, fusion of the colloid droplets with the lysosomes, digestion of thyroglobulin by a cathepsin, dehalogenation of tyrosines and release of thyronines into the blood stream. The present paper describes a double isotope technique for studying the first two steps. Thyrotrophin (TSH) administration to rats increased the radioactivity present in all fractions, specially in the 15 000 × g pellet. When the subcellular distribution of acid phosphatase was determined, the highest specific activity was found in this fraction, thus indicating the presence of lysosomes. The content of radioactive materials in the 15 000 × g pellet was analyzed by trichloroacetic acid precipitation and by ascending paper chromatography using n-butanol:ethanol:ammonium hydroxide (5:1:2;v/v) as solvent system. The results obtained showed that 90% of the radioactivity was protein bound and strongly suggest that this material is thyroglobulin.


2021 ◽  
Vol 1825 (1) ◽  
pp. 012071
Author(s):  
Hendri Widiyandari ◽  
Shabrina Hayu Adhani ◽  
Agus Subagio ◽  
Agus Purwanto

1978 ◽  
Vol 31 (3) ◽  
pp. 209 ◽  
Author(s):  
TC Elleman ◽  
IR Falconer ◽  
ARB Jackson ◽  
MT Runnegar

The nature of the toxicity of a bloom of blue-green alga, M. aeruginosa (= Anacystis cyanea), that occurred in a man-made lake was investigated. Crude algal bloom extracts were toxic to laboratory mice when injected intraperitoneaIIy. The lethal dose (LDlOO) of these extracts was 15-30 mg of lyophilized algal bloom per kilogram body weight. The toxin was purified by a procedure that included ammonium sulphate fractionation, solvent extraction, acid precipitation, Sephadex G25 and DEAE-Sephadex chromatography, and high-voltage electrophoresis at pH 6�5. The preparation gave a single spot on high-voltage electrophoresis at pH 9�0, had no free amino group, and was characterized by a simple amino acid composition of equimolar quantities of L-methionine, L-tyrosine, D-alanine, D-glutamic acid, erythro fi-methyl aspartic acid and methylamine.


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