STRUCTURAL COMPARISON OF RECOMBINANT PULMONARY SURFACTANT PROTEIN SP-A DERIVED FROM 2 HUMAN CODING SEQUENCES - IMPLICATIONS FOR THE CHAIN COMPOSITION OF NATURAL HUMAN SP-A

被引：106

作者：

VOSS, T ^{[1
]}

MELCHERS, K ^{[1
]}

SCHEIRLE, G ^{[1
]}

SCHAFER, KP ^{[1
]}

机构：

[1] BYK GULDEN LOMBERG GMBH,DEPT MOLEC BIOL,GOTTLIEBER STR 25,W-7750 CONSTANCE,GERMANY

来源：

AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY | 1991年 / 4卷 / 01期

关键词：

D O I：

10.1165/ajrcmb/4.1.88

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The pulmonary surfactant-associated protein SP-A is encoded by presumably two different genes, resulting in slightly different amino acid sequences. Both gene products were expressed in Chinese hamster ovary cells. Their macromolecular structure differed significantly. SP-A-alpha-3 exhibited a much higher amount of tetrameric to hexameric structures than SP-A-alpha-2, for which dimeric structures predominate. These differences may be caused by the higher expression rates of SP-A-alpha-3 presumably due to the presence of introns in the sequence. The occurrence of irregular disulfide links between individual oligomeric SP-A molecules composed of alpha-3-chains together with the demonstrated presence of both gene products in natural human SP-A suggest that the subunits of SP-A are heterotrimers of one alpha-2- and two alpha-3-chains.

引用

页码：88 / 94

页数：7