| Literature DB >> 9027993 |
J Delfín1, I Martínez, W Antuch, V Morera, Y González, R Rodríguez, M Márquez, A Saroyán, N Larionova, J Díaz, G Padrón, M Chávez.
Abstract
Isolation of proteinase inhibitors from the sea anemone Stichodactyla helianthus was achieved by trichloroacetic acid treatment of the aqueous extract followed by affinity chromatography on trypsin-Sepharose and ion-exchange chromatography on CM-cellulose. The average molecular mass of the major inhibitor (ShPI-I) obtained by fast atom bombardment mass spectrometry (FAB-MS) was 6110.6 Da. The amino acid sequence was determined by FAB-MS combined with manual Edman degradation, digestions with endopeptidases and exopeptidases and automatic sequencing. The sequence of ShPI-I (55 amino acids) was compared with those reported in the SwissProt database for several proteinase inhibitors and significant similarity to inhibitors belonging to the Kunitz family was observed. ShPI-I exhibits a broad specificity for serine, cysteine and aspartic proteinases. The dissociation constants of the complexes formed with different enzymes were determined. The affinity-purified fraction (PI) was immobilized on Sepharose and used in the purification of different classes of proteinases.Entities:
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Year: 1996 PMID： 9027993 DOI： 10.1016/s0041-0101(96)00114-6
Source DB: PubMed Journal: Toxicon ISSN： 0041-0101 Impact factor: 3.033