Amino acid composition and N-terminal sequence of purified Cystine Binding Protein of Escherichia coli

• Published in: Life sciences (1973) Vol. 52; no. 14; pp. 1209 - 1215
• Main Authors: Butler, Jean DeBrohun, Levin, Sondra Warren, Facchiano, Antonio, Miele, Lucio, Mukherjee, Anil B.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 1993; Elsevier
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Analytical, structural and metabolic biochemistry; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding and carrier proteins; Biological and medical sciences; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Chromatography, High Pressure Liquid; Cystine - metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli - chemistry; Escherichia coli Proteins; Fundamental and applied biological sciences. Psychology; Molecular Sequence Data; Proteins; Binding protein; Aminoacid; Escherichia coli; N terminal-Sequence; Bacteria; Chemical composition; Carrier protein; Enterobacteriaceae; Cystine
• ISSN: 0024-3205; 1879-0631
• DOI: 10.1016/0024-3205(93)90103-A

Cystine Binding Protein (CBP), a commercially available crude protein extract obtained by osmotic shock of Escherichia coli (E. coli), was studied to characterize further its cystine binding properties and to elucidate its cystine transport activity. We report here the amino acid composition, the N-terminal amino acid sequence analysis and some binding characterics of the purified cystine binding component of CBP. A search of the Swiss-Prot version 20 data base revealed that this sequence is unique.