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: Preliminary X-ray diffraction studies and biochemical characterization of the antitumor protein mitomalcin indicate close similarity to neocarzinostatin.
    Author: Sieker LC, Gnanarajah GG.
    Journal: Proteins; 1988; 3(4):252-5. PubMed ID: 2971216.
    Abstract:
    The antitumor antibiotic protein mitomalcin, from the microorganism Streptomyces malayensis, has been purified to apparent homogeneity and crystallized. The crystals belong to space group P2(1)2(1)2(1) and have the following cell parameters: a = 27.2 A, b = 34.1 A, c = 101.7 A, and alpha = beta = gamma = 90 degrees. These crystal properties are extremely similar to crystals of the antitumor protein neocarzinostatin (11.7 kilodaltons [kDa]) from Streptomyces carzinostaticus in spite of differing pH conditions for crystallizing the two proteins and an apparent difference in molecular weight. Gel electrophoresis shows the molecular weight is similar to that of neocarzinostatin. An amino acid composition analysis of mitomalcin indicates that some differences may exist between the two molecules, but a preliminary amino acid sequence analysis of the first 37 residues found no difference in the N-terminal region of the molecule.
    [Abstract] [Full Text] [Related] [New Search]