Proteolytic Activity In Adult Haemonchus Contortos

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dc.contributor.advisorOduro, K.K.
dc.contributor.authorSackey, S. T
dc.contributor.otherUniversity of Ghana, College of Basic and Applied Sciences, School of Biological Sciences, Department of Biochemistry, Cell and Molecular Biology
dc.date.accessioned2015-10-20T10:34:25Z
dc.date.accessioned2017-10-13T17:02:38Z
dc.date.available2015-10-20T10:34:25Z
dc.date.available2017-10-13T17:02:38Z
dc.date.issued1982
dc.descriptionThesis(MSc)-University of Ghana,1982.en_US
dc.description.abstractProteolytic activity of the JQ.qOOxgsupernate of homegenates ef adult Haemonchus contortus has been studied with respect to substrates susceptible to its proteolytic activity, and the effects of factors such as temperature, pH, substrate concentration, extract concentration, dibasic metal ions, detergents, heat and some specific inhibitors of proteolytic activity. The supernate had two pH optima, 5.6 with haemoglobii as substrate, and 7.8 using L-alanyl - p-nitroanilide. It showed optimum activity at 36°C, was heat labile and in general was not significantly affected by the presence of metal ions in the hydrolysis of haemoglobin and L-alanyl p-nitroanilide. In screening for substrates susceptible to its hydrolytic action the most suitable were found to be those p-nitroanilides and jp-naphthylamides which have a single amino acid group (small R-group), unprotected at the free functional group end. The kinetic studies indicated that haemoglobin was more rfeadily hydrolysed than the p-nitroanilides and p-naphthylamides.en_US
dc.format.extentx, 75p.
dc.identifier.urihttp://197.255.68.203/handle/123456789/7025
dc.language.isoenen_US
dc.publisherUniversity of Ghanaen_US
dc.rights.holderUniversity of Ghana
dc.titleProteolytic Activity In Adult Haemonchus Contortosen_US
dc.typeThesisen_US

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