The role of the carbohydrate moiety for the inhibitory activity of antithrombin III

Schiele, Ulrike; Heuck, C C

doi:10.1016/0049-3848(85)90130-6

Cited by 3 publications

(1 citation statement)

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“…This again might be caused by an aberrant pattern of sugar moieties in the recombinant antithrombin III. As mentioned above, some of the antithrombin I I I activities seem to be very sensitive even to subtle changes in its carbohydrate side chains (Peterson et al 1985;Schiele and Heuck 1985).…”

Section: Discussionmentioning

confidence: 99%

Expression of human antithrombin III in the cellular slime mould Dictyostelium discoideum

Dingermann

Troidl

Bröker

et al. 1991

Appl Microbiol Biotechnol

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In order to test the biotechnological potential of the cellular slime mould Dictyostelium discoideum the cDNA coding for human antithrombin III was expressed in this microorganism. The 1392-bp antithrombin III cDNA was fused to the N-terminal coding part of the D. discoideum actin 6 gene. In constructs carrying this artificial N-terminal coding region only low amounts of antithrombin III were detected. However, constructs from which all actin coding nucleotides were removed produced significant amounts of anti-thrombin III, most of which was secreted into the culture broth. Stationary cultures (1.5 x 10(7) cells/ml) of certain stable transformants accumulated up to 1.0 microgram antithrombin III/ml culture medium within 24 h. The recombinant protein has a slightly smaller molecular weight in sodium dodecyl sulphate-polyacrylamide gels than authentic plasma antithrombin III and it is glycosylated, as determined by concanavalin A labelling.

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Section: Discussionmentioning

confidence: 99%