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The authors discuss technical and human performance issues associated with using speech recognition technology in the telephone network, as well as methods for minimizing the associated problems. In particular, motivations and methodologies for using the technology as part of the process of automating the verification of collect and third number billed calls are discussed. The criteria for a speech recognition system for this and other telephone network applications and the shortcomings of the current technology, as well as how to optimize the technology given the current constraints, are explained. Issues for the vendor community to be aware of regarding the use of the technology in the telephone network are identified in order to encourage a concerted effort that would result in the optimization of speech recognition technology as it applies to alternate billing services and other types of automation. >

A male inhibitory material (HuSePl-Frl) was separated from normal human seminal plasma by gel filtration on Sephadex G-100. This material has high avidity for cell membranes of human red blood cells (RBC). In vitro, PHA-M-induced blast transformation of human lymphocytes is inhibited by small quantities of HuSePl-Frl. This inhibition was also evident when RBC coated with HuSePl-Frl is added to mitogen stimulated lymphocytes in cultures. Small quantities of HuSePl-Frl are inhibitory to natural killer (NK) cell activation. The modulating role of the HuSePl-Frl in preventing the spermatozoal rejection during fertilization is discussed.

1. 1. An enzyme sysetm obtained from baker's yeast converted 2-methyl-4 amino-5-aminomethylpyrimidine to 2-methyl-4-amino-5-hydroxymethylpyrimidine, a known intermediate in thiamine biosynthesis. The pH optimum of the system was 7.8 and the apparent Km value for the substrate was 5·10−5 M. The enzyme system was inhibited by 2-mercaptoethanol, pyridoxal phosphate, the amine oxidase inhibitors pargyline and tranylcypromine, and by various carbonyl reagents and chelating agents. 2. 2. Enzymes systems catalyzing a similar reaction were reaction were found to be present in Neurospora crasa extracts and in a crude preparation of Bacillus thiaminolyticus thiaminase.

Paper chromatography, descending, using the solvent system: n-butanol: acetic acid: water (8: 1: 1. v/v) separated semen components which supported growth of a carnitine-requiring mutant of the yeast. Torulopsis bovina. These chromatographic zones contained free L-carnitine. its acetyl and propionyl esters, esters with 4-carbon acids and the amino acid arginine.

Publisher Summary This chapter describes the measurement of carnitine and o -acylcarnitines. Carnitine is shown to be essential for β-oxidation of long-chain fatty acids in mammalian system. The assays for carnitine are based on the reaction catalyzed by carnitine acetyltransferase. The sensitivity of the enzymatic method was greatly increased by the introduction of a radioisotopic assay that depends on the incorporation of the acetyl moiety of [1- 14 C]acetyl-CoA into acetylcarnitine followed by separation and measurement of the amount of [ 14 C]acetylcarnitine formed. The growth rate of a carnitine-requiring mutant of the yeast Torulopsis bovina can be dependent on the carnitine content of the growth medium when cultures are grown under strictly defined conditions. The quantitation of short-chain acylcarnitines by gas chromatography is explained. The method depends on separating water-soluble acylcarnitines from other acyl-containing compounds and then saponifying the acylcarnitines and quantitating the individual fatty acids by gas chromatography. The quantitative enzymatic assay of short-chain acylcarnitines after separation by paper chromatography is also discussed.

Esters of carnitine with fatty acids containing two to five carbon atoms were separated by descending chromatography on Whatman No. 1 paper, using the solvent system, n-butanol: acetic acid:water (8:1:1, v/v). The separated derivatives were hydrolyzed with ammonia; the resulting l -carnitine was eluted from each chromatographic zone and assayed enzymatically. This procedure permits separation and assay of nanomole amounts of acylcarnitines from biological materials.

Inositol phosphatide has been obtained from raw peas of all stages of maturity, excluding dry seed peas, after the peas were held in frozen storage (−17.8 °C.) for several months. The liberation is believed to be enzymic in nature. Peas which had been heat treated to inactivate enzymes yielded negligible amounts of inositol phosphatide. Silicic acid-impregnated paper chromatography confirmed the presence of inositol phosphatide, and silicic acid chromatography showed its heterogeneity. The analytical data have been supplemented by analyses for inositol and fatty acids. Some discussion has been presented concerning the purity and composition of this fraction of pea lipides.

1. 1. Cell-free preparations of Saccharomyces cerevisiae, were shown to catalyze the reduction of 2-methyl-4-amino-5-formylpyrimidine to the corresponding 5-hydroxymethyl derivative, a known intermediate in thiamine biosynthesis. Either NADH or NADPH served as a cofactor. The pH optimum of the system was 6.5–7.0 and the apparent Km for the formylpyrimidine substrate was 3.3·10−4 M. 2. 2. Details of a microbiological assay for the pyrimidine moiety of thiamine, using Escherichia coli Strain M70-17, are described.