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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
361

New routes to imino sugars

Dransfield, Paul John January 2002 (has links)
No description available.
362

Isolation, purification and characterisation of a novel lysozyme from a rumen ciliate Entodinium caudatum

Martin, Heather Christine January 1999 (has links)
The rate of breakdown of a range of rumen bacteria by rumen protozoa in whole rumen fluid ranged from 11.5%/h for <I>Butyrivibrio fibrisolvens</I> SH13 to 2.7%/h for <I>Eubacterium ruminantium </I>2388. When the rates of breakdown of the bacteria were measured using hen's egg white lysozyme, an N-acetylmuramidase, they ranged from 10.1%/h to 1.1%/h. There was correlation between levels of activity in lysozyme and rumen fluid, with R<SUP>2</SUP>=0.52 (P>0.01). The rates of breakdown of the rumen bacteria using mutanolysin, also an N-acetylmuramidase<I> </I>were also measured. They ranged from 16.0 to 1.2%/h, and the R<SUP>2</SUP> value was 0.81. When the same bacteria were incubated with an N-acetylglucosaminidase, the rates of breakdown ranged from 3.9 to 0.27%/h, and there was no correlation with the activity in rumen fluid. This implied that the principal bacteriolytic activity in rumen fluid is similar to lysozyme (EC 3.2.1.17). Protozoal lysozyme was partially purified from <I>Entodinium caudatum</I> using a combination of cation exchange and gel filtration chromatography. The partially-purified enzyme resembled other lysozymes in that it was a basic protein which degraded <I>Micrococcus lysodeikticus</I> cell walls and had a high isoelectric point of pI9. It displayed optimal activity at pH 6.5, ionic strength of 0.05 M and at a temperature of 40 °C. It had an apparent affinity constant (K<I><SUB>app</SUB></I>) of 388 mg <I>M. lysodeikticus</I> lysed/I. It had an apparent molecular mass of 14 kDa, from SDS-PAGE, and its N-terminal amino acid sequence slightly resembled that of a distinct class of lysozymes found in <I>Streptomyces</I> species, the fungus <I>Chalaropsis </I>and the protozoan parasite <I>Entamoeba histolytica</I>. Thus the major type of bacteriolytic activity in rumen fluid was found to be a lysozyme-like enzyme which was partially purified and characterised. Further characterisation of this enzyme could provide important information that would be useful in developing a means of preventing wasteful breakdown of bacterial protein in the rumen.
363

Purification and characterization of prokallikrein from bovine pancreas

Al-Hamidi, Abdulaziz Abdullah Abdulrahman January 1990 (has links)
No description available.
364

A study of chymotrypsins and carboxypeptidase B from camel pancreas

Al-Ajlan, Abdulrahman S. M. January 1999 (has links)
No description available.
365

The production of cytochrome P-450 by Saccharomyces cerevisiae during computer-controlled batch fermentations

Dorr, Arthur January 1991 (has links)
No description available.
366

Isolation, characterisation and expression of cDNAs coding for rat and human kidney cysteine conjugate #beta#-lyase

Hill, Sandra Jane January 1995 (has links)
No description available.
367

Approaches to selective synthesis using modified enzyme systems

Aitken, D. J. January 1987 (has links)
No description available.
368

Aldo-keto reductases of the yeast Saccharomyces cerevisiae

Ford, Gordon January 2001 (has links)
No description available.
369

A comparative study of the interaction between the conversion factor from human tissues with the small forms of adenosine deaminase from various organisms

Puttaswamy, Shashi January 1981 (has links)
Two molecular forms of adenosine deaminase have been isolated from bovine livers. These two forms were found to be interconvertible. Adenosine deaminase extracted from human tissues exhibited similar properties as well. Previous studies have shown the presence of a conversion factor which formed an aggregate with the small form (the C-form) of the enzymes, and the resulting enzyme complex was identified to be the large form (the A-form) of adenosine deaminase. Studies have been made with rat tissues. The C-form of the adenosine deaminase is widely distributed in the various tissues, while the large form of the enzyme is absent in those tissues examined.The outline of this study is summarized below: (1) The isolation of the conversion factor from human liver.(2) The isolation of the adenosine deaminase from the various tissues.(3) The coversion of human adenosine deaminase C-form to the A-form.(4) Quantization of the conversion of the C-form to the A-form.(5) Testing the effect of conversion on nonhuman enzymes.(6) The optimum temperature and time to yield greatest amount of conversion.The results from this study would verify any differences that might exist between the small forms of the enzyme present in different species.
370

A denaturant-stable protease isolated from pronase : qualitative comparisons of the cleavage specificities in the presence and absence of denaturant

Lindley, Brenda Rae January 1982 (has links)
Guanidine-stable chymoelastase (GSC-Elastase), an enzyme isolated from a commercial protease preparation (Pronase), has been shown to be stable and active in the presence of 6.0 M guanidinium chloride (Si egel , S . , et. al . , J . Biol. Chem. 247:4155, J . Pi of . Chem. 248:3233.) The amino acid sequence around the active site serine residue for the protease is similar to that found for bovine chymotrypsin (Awad, W. M. et.al., J. Biol. Chem. 247:4144). This investigation involved the qualitative comparison of the protein cleavage specificity of GSC-Elastase in the presence and absence of denaturant. This specificity was also compared to that found for a-chymotrypsin for the existence of possible similarities in their actionson protein substrates. S-Carboxymethylated lysozyme (CM-HEL) was hydrolyzed in separate trials which were catalyzed by GSC-Elastase in the presence and absence of 6.0 M guanidinium chloride and by a-chymotrypsin. Two-dimensional peptide maps were made from each of the hydrolysates by performing thin-layer chromatography in one direction followed by electrophoresis in a perpendicular direction. The results of the mapping procedure indicated that the cleavage of protein substrates by GSC-Elastase is reproducible and therefore specific under denaturing conditions as well as in the absence of denaturant. These results also suggested that the protein cleavage specificity of GSC-Elastase was found to be significantly different from that of bovine chymotrypsin.

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