These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Design of an aprotinin variant with inhibitory activity against chymotrypsin and cathepsin G by recombinant DNA technology.
    Author: Brinkmann T, Tschesche H.
    Journal: Biol Chem Hoppe Seyler; 1990 May; 371 Suppl():43-52. PubMed ID: 1698068.
    Abstract:
    The [Phe15,17, Glu52]aprotinin gene was constructed from synthetic [Glu52]aprotinin gene by DNA cassette mutagenesis. For substitution of the P1, P'1, P'2 residues of aprotinin (Lys15-Ala16-Arg17) two complementary synthetic oligonucleotides including a new segment coding for the Phe15-Ala16-Phe17 sequence were inserted into the expression vector. The expression was carried out in an E. coli host and [Phe15,17, Glu52]aprotinin was obtained as fusion protein with bacteriophage MS2 polymerase and deposited in inclusion bodies. After CNBr cleavage and renaturation of aprotinin on CM Sepharose Fast Flow the active aprotinin variant was isolated and its specificities investigated. The new [Phe15,17, Glu52]aprotinin was shown to be an inhibitor for bovine chymotrypsin (Ki = 6.5 x 10(-10)M) essentially identical to the previously prepared semisynthetic [Phe15]aprotinin (Ki = 2.0 x 10(-10)M) (1). However, the new variant exhibited an additional inhibitory activity against cathepsin G from human leukocytes (Ki = 5.0 x 10(-7)M) in contrast to semisynthetic [Phe15] variant which was inactive.
    [Abstract] [Full Text] [Related] [New Search]