Abstract：
:A polypeptide coded as PGC was isolated from Arca subcrenata muscle using ion exchange, Sephadex G-50 gel chromatography and RP-HPLC. PGC was identified to be a homogeneous compound by Native-PAGE and the purity was more than 98.9% measured by HPLC. The isoelectric point of PGC was determined to be 9.76 by IEF-PAGE. The molecular weight was determined to be 15,973.0Da by ESI-MS/MS. The conformational structure of PGC was characterized by UV-vis, FT-IR and CD spectroscopy. N terminal amino acid sequence of PGC was shown as PSVYDAAAQLTADVKKDLRDSWKVIGGDKKGNGVA by Edman degradation. The results demonstrated that there is a high degree of homology between PGC and the subunit from hemoglobin, and proposed that PGC is the depolymerized polypeptide of Hemoglobin I (HbI) from A. subcrenata. The evaluation of biological activities showed that the diameters of the inhibitory ring of PGC on Escherichia coli and Staphylococcus aureus were 14.5±0.44mm and 16.5±1.15mm, respectively. The IC50 of inhibition rate for PGC on NO production was 9.60±0.71μg/mL. Therefore, PGC might be developed as one of potential antibacterial and anti-inflammatory agents.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Chen Y,Li C,Zhu J,Xie W,Hu X,Song L,Zi J,Yu Rdoi
10.1016/j.ijbiomac.2016.11.082subject
Has Abstractpub_date
2017-03-01 00:00:00pages
177-184eissn
0141-8130issn
1879-0003pii
S0141-8130(16)31031-5journal_volume
96pub_type
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