The activation of pepsinogen.

dc.contributor.author	Yuan, Larry Chi-Yang.
dc.date.accessioned	2009-04-17T16:00:13Z
dc.date.available	2009-04-17T16:00:13Z
dc.date.created	1963
dc.date.issued	1963
dc.degree.level	Doctoral
dc.description.abstract	The activation of purified pepsinogen was studied at pH 2.0 and 5.6 and at 20°C and 0°C. It was found to be catalyzed by hydrogen ions at pH 2.0 and to be truly autocatalytic only at pH 5.6 and 0°C. A certain number of peptides produced during activation were isolated, the rate of formation of the main peptide was found to be identical with the rate of formation of pepsin. The production of the other important peptides could be explained only by assuming that more than one species of active pepsin is produced during activation. It is concluded that the production of each species of active pepsin involves the cleavage of only one peptide bond in each case.
dc.format.extent	76 p.
dc.identifier.citation	Source: Dissertation Abstracts International, Volume: 68-06, Section: B, page: 3778.
dc.identifier.uri	http://hdl.handle.net/10393/10677
dc.identifier.uri	http://dx.doi.org/10.20381/ruor-8407
dc.publisher	University of Ottawa (Canada)
dc.subject.classification	Chemistry, Biochemistry.
dc.title	The activation of pepsinogen.
dc.type	Thesis

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