Show simple item record

dc.contributor.authorLuo Lian-Zhong
dc.contributor.author罗联忠
dc.contributor.authorJin Hong-Wei
dc.contributor.author金宏伟
dc.contributor.authorCai Zong-Wei
dc.contributor.author蔡宗苇
dc.contributor.authorHuang He-Qing
dc.contributor.author黄河清
dc.date.accessioned2012-03-18T04:56:37Z
dc.date.available2012-03-18T04:56:37Z
dc.date.issued2011
dc.identifier.citationCHINESE JOURNAL OF ANALYTICAL CHEMISTRY,2011,39(2):155-162zh_CN
dc.identifier.issn0253-3820
dc.identifier.urihttp://dx.doi.org/doi:10.3724/SP.J.1096.2011.00155
dc.identifier.uriWOS:000290240800001
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/11783
dc.description.abstractAs an experimental material of human placental tissue, membrane ferritin of human placenta (HPMF) with electrophoresis purity was prepared in batch. SDS-PAGE approach reveals that the protein shell consists of double subunits of a type in HPMF, which the molecular weights of both subunits were calculated to be approximately 15 and 20 kDa respectively, named MF(15) and MF(20). In addition, the protein content of MF(15) is about three times more than that of M(20) in SDS- PAGE gel. Using the approach of peptide mass fingerprinting (PMF), both MF(15) and MF(20) subunits were identified to show the high homology with reference to L subunit of human ferritin, pointing out that HPMF was a novel ferritin of two subunits involving in single type and different molecular weight. Using a matrix-assisted laser desorption ionization time of flight mass spectrometry to investigate the subunit-stability of HPMF, five mass peaks corresponding ratio (m/z) of mass to charge such as 5071. 25, 9962. 51, 15131. 55 (MF(15)), 19936. 40 (MF(20)) and 20147. 61 were indicated to have five subunit formula of [MF(15)](3+), [MF(20)](2+), [MF,](+), [MF(20)](+) and [MF(20+Fe)](+) respectively. Using inductively coupled plasma-mass spectrometry to analyze the elemental composition of HPMF, only 85 Fe(3+) and 15 inorganic phosphate (P(i)) in the iron core of per molecular of HPMF were found, which was significantly lower than that of most mammal ferritins, but higher than that of bacterial ferritin (BF). Kinetic studies showed that iron release from the complete HPMF followed the law with first-order reaction, which also differed from that with two different rates in mammal ferritins. In addition, the time of the iron release completely needed about 750 min in human placental membrane ferritin (HPMF), which was longer than 60 min in both horse spleen ferritin (HSF) and pig pancreatic ferritin (PPF). Accordingly, based on the difference of structure and function among HPMF, mammalian ferritins, plant ferritins, and BF, we proposed M(15) and M(20) subunit play different role in iron transporting from maternal blood to fetal blood.zh_CN
dc.language.isozhzh_CN
dc.publisherELSEVIER SCIENCE INCzh_CN
dc.subjectHuman placental member ferritinzh_CN
dc.subjectSingle subunit typezh_CN
dc.subjectSubunit functionzh_CN
dc.subjectIron transporting modelzh_CN
dc.subjectStructure and functionzh_CN
dc.titleFunctions of Double Subunits of a Type, Structure of Iron Corn, and Kinetics of Iron Release from Membrane Ferritin of Human Placentazh_CN
dc.typeArticlezh_CN


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record