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Purification and phosphorylation of the intact form of complement component C4 from human plasma
2000 (Swedish)Independent thesis Basic level (degree of Bachelor)Student thesis
Abstract [en]

A casein kinase released from activated human platelets has been shown to phosphorylate a number of plasma proteins. When platelets are activated they release substantial amounts of ATP and divalent cations which are necessary for phosphorylation of proteins. The aim of this study was to elucidate the optimal conditions for phosphorylation of the human complement component C4, identify phosphorylation site in the molecule and to investigate possible impact on the functions of phosphorylated C4. For this purpose, C4 must be prepared from human plasma, which was done using a modification of a previously published method. The results showed a pure and 100 % active protein. C4 was incubated with [g-32P]ATP and cations. After SDS-PAGE and autoradiography it was shown that C4 was phosphorylated in the a-chain. Maximal phosphorylation was achieved when C4 was phosphorylated in the presence of 20 mM Ca2+. Incubation of phosphorylated and unphosphorylated C4 with trypsin showed that phosphorylated C4 was less susceptible to cleavage by trypsin than unphosphorylated. In contrast, phosphorylation did not affect the cleavage of C4 by Factor I. Furthermore, no difference was seen when phosphorylated and unphosphorylated C4 was incubated with [2-3H]glycine and [2-3H]glycerol. Glycerol and glycine were bound to both phosphorylated and unphosphorylated C4 to the same extent, indicating that phosphorylation does not affect the ability of C4 to form amide or ester bonds.

Place, publisher, year, edition, pages
2000. , 36 p.
Identifiers
URN: urn:nbn:se:kau:diva-52404Local ID: KEM-10OAI: oai:DiVA.org:kau-52404DiVA: diva2:1100930
Subject / course
Chemistry
Available from: 2017-05-29 Created: 2017-05-29

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