Van Hoozen C M, Ling E H, Halsted C H
Division of Clinical Nutrition and Metabolism, School of Medicine, University of California, Davis 95616, USA.
Biochem J. 1996 Nov 1;319 ( Pt 3)(Pt 3):725-9. doi: 10.1042/bj3190725.
Folate-binding protein (FBP) was identified and characterized in a pig liver cDNA library by screening with a 0.6 kb fragment from the cDNA of FBP from a human KB cell cancer line. The cDNA of pig liver FBP included 1230 bp containing 759 bp in the open reading frame with 80% similarity to the human placenta FBP. The deduced 253 amino acid sequence showed 67-73% similarity to previous sequences and contained 16 conserved cysteine residues, 11 tryptophan potential folate-binding sites, three sites for N-linked glycosylation and 14 hydrophobic C-terminal residues. Northern analysis and reverse transcriptase PCR identified transcripts in pig liver and kidney, but not in jejunal mucosa. Although defining the molecular structure of pig liver FBP, these studies suggest that this protein participates in the regulation of folate uptake by liver and kidney membranes but is not involved in folate absorption.
通过用人KB细胞癌细胞系FBP cDNA的0.6 kb片段进行筛选,在猪肝cDNA文库中鉴定并表征了叶酸结合蛋白(FBP)。猪肝FBP的cDNA包含1230 bp,其中开放阅读框中有759 bp,与人胎盘FBP的相似性为80%。推导的253个氨基酸序列与先前序列的相似性为67%-73%,包含16个保守的半胱氨酸残基、11个潜在的叶酸结合色氨酸位点、3个N-糖基化位点和14个疏水的C末端残基。Northern分析和逆转录酶PCR在猪肝和肾中鉴定出转录本,但在空肠黏膜中未鉴定出。尽管确定了猪肝FBP的分子结构,但这些研究表明该蛋白参与肝脏和肾脏膜对叶酸摄取的调节,但不参与叶酸吸收。