Show simple item record

Files in this item

Thumbnail

Item metadata

dc.contributor.advisorKemp, Graham D.
dc.contributor.authorPejhan, Nooshabeh
dc.coverage.spatial173 p.en_US
dc.date.accessioned2018-07-05T09:09:15Z
dc.date.available2018-07-05T09:09:15Z
dc.date.issued1984
dc.identifier.urihttp://hdl.handle.net/10023/14960
dc.description.abstractAn attempt has been made to purify an acid proteinase from human plasma, which is capable of dissolving fibrin clot in 1% (w/v) monochloroacetic acid. On SDS gel electrophoresis the enzyme isolated from plasma contains two protein bands with molecular weights of approximately 90,000 and 54,000. Different substrates were used to evaluate the proteolytic activity of the plasma enzyme, including fibrin clot, azo-casein, acid denatured haemoglobin (Hb), haemoglobin polyacrylamide gel (insoluble Hb), haemoglobin electrophoresis (soluble Hb) and the synthetic substrate N-acetyl-L-phenylalanyl-L-diiodotyrosine. The plasma enzyme seems to belong to the group of aspartyl proteinases as its activity against the above substrates was maximal at low pH, and was inhibited by pepstatin which is a powerful inhibitor of aspartyl proteinases.en_US
dc.language.isoenen_US
dc.publisherUniversity of St Andrews
dc.subject.lccQP92.3P3
dc.subject.lcshFormation--Hematopoiesis--Bone marrowen
dc.titleA fibrinolytic acid proteinase in human plasmaen_US
dc.typeThesisen_US
dc.type.qualificationlevelDoctoralen_US
dc.type.qualificationnamePhD Doctor of Philosophyen_US
dc.publisher.institutionThe University of St Andrewsen_US


This item appears in the following Collection(s)

Show simple item record