Unknown

Dataset Information

0

Induction of apoptotic effects of antiproliferative protein from the seeds of Borreria hispida on lung cancer (A549) and cervical cancer (HeLa) cell lines.


ABSTRACT: A 35 KDa protein referred to as F3 was purified from the seeds of Borreria hispida by precipitation with 80% ammonium sulphate and gel filtration on Sephadex G-100 column. RP-HPLC analysis of protein fraction (F3) on an analytical C-18 column produced a single peak, detected at 220?nm. F3 showed an apparent molecular weight of 35?KDa by SDS PAGE and MALDI-TOF-MS analyses. Peptide mass fingerprinting analysis of F3 showed the closest homology with the sequence of 1-aminocyclopropane-1-carboxylate deaminase of Pyrococcus horikoshii. The protein (F3) exhibited significant cytotoxic activity against lung (A549) and cervical (HeLa) cancer cells in a dose-dependent manner at concentrations ranging from 10?µg to 1000?µg/mL, as revealed by the MTT assay. Cell cycle analysis revealed the increased growth of sub-G0 population in both cell lines exposed to a concentration of 1000?µg/mL of protein fraction F3 as examined from flow cytometry. This is the first report of a protein from the seeds of Borreria hispida with antiproliferative and apoptotic activity in lung (A549) and cervical (HeLa) cancer cells.

SUBMITTER: Rupachandra S 

PROVIDER: S-EPMC3925513 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

Induction of apoptotic effects of antiproliferative protein from the seeds of Borreria hispida on lung cancer (A549) and cervical cancer (HeLa) cell lines.

Rupachandra S S   Sarada D V L DV  

BioMed research international 20140130


A 35 KDa protein referred to as F3 was purified from the seeds of Borreria hispida by precipitation with 80% ammonium sulphate and gel filtration on Sephadex G-100 column. RP-HPLC analysis of protein fraction (F3) on an analytical C-18 column produced a single peak, detected at 220 nm. F3 showed an apparent molecular weight of 35 KDa by SDS PAGE and MALDI-TOF-MS analyses. Peptide mass fingerprinting analysis of F3 showed the closest homology with the sequence of 1-aminocyclopropane-1-carboxylate  ...[more]

Similar Datasets

| S-EPMC6273349 | biostudies-literature
| S-EPMC6222523 | biostudies-literature
| S-EPMC7076859 | biostudies-literature
| S-EPMC7194401 | biostudies-literature
| S-EPMC6445431 | biostudies-literature
| S-EPMC8879438 | biostudies-literature
| S-EPMC7412766 | biostudies-literature
| S-EPMC8838532 | biostudies-literature
| S-EPMC10439542 | biostudies-literature
| S-EPMC6000036 | biostudies-literature