Far Western

An interaction is detected between a protein immobilized on a membrane and a purified protein probe.

Publication

The p11 subunit of annexin II heterotetramer is regulated by basic carboxypeptidase.

Fogg DK, Bridges DE, Cheung KK, Kassam G, Filipenko NR, Choi KS, Fitzpatrick SL, Nesheim M, Waisman DM

The Ca(2+)-dependent phospholipid-binding protein annexin II heterotetramer (AIIt) is composed of two copies of annexin II and a p11 dimer. The interaction of the carboxyl-terminal lysine residues of the p11 subunit of AIIt with the lysine-binding kringle domains of plasminogen is believed to play a key role in plasminogen binding and stimulation of the tPA-catalyzed cleavage of plasminogen to plasmin. ... [more]

Biochemistry Apr. 16, 2002; 41(15);4953-61 [Pubmed: 11939791]

Throughput

  • Low Throughput

Curated By

  • BioGRID