EurekaMag.com logo
+ Translate

The primary structure of leucine iso leucine valine binding protein from escherichia coli 3. the peptides of restricted tryptic and limited acidic hydrolysis determination of a di sulfide bridge in the protein molecule


, : The primary structure of leucine iso leucine valine binding protein from escherichia coli 3. the peptides of restricted tryptic and limited acidic hydrolysis determination of a di sulfide bridge in the protein molecule. Bioorganicheskaya Khimiya 6(1): 31-45

Tryptic hydrolysis of carboxymethylated, maleylated Leu, Ile, Val (LIV)-binding protein from E. coli was performed. By gel-filtration, DEAE-chromatography and paper chromatography, 8 individual peptides were isolated. The complete structures of 6 peptides and partial amino acid sequences of 2 peptides were determined. Acidic hydrolysis at Asp-Pro bonds reslted in 4 fragments, which were resolved by gel-filtration and DEAE-chromatography. The structural analysis of the obtained peptides allowed to complete the reconstruction of the polypeptide chain of the protein. The presence of a disulfide bridge in the LIV-protein was established by 2 different methods.

(PDF 0-2 workdays service)

Accession: 006740935

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Anonymous, 1980: Primary structure of the leucine iso leucine valine binding protein from escherichia coli 3 peptides from selective tryptic and limited acid hydrolyses determination of the di sulfide bridge in the protein molecule

Grinkevich, V.A.; Arzamazova, N.M.; Potapenko, N.A.; Grinkevich-Kh, A.; Kravchenko, Z.B.; Feigina, M.Y. ; Aldanova, N.A., 1979: Primary structure of leucine iso leucine valine binding protein from escherichia coli 1. the peptides of exhaustive tryptic hydrolysis. Exhaustive tryptic digestion of carboxymethylated Leu, IIe, Val (LIV)-binding protein was performed. For the initial separation of hydrolysate, chromatography on Aminex AG 50W .times. 4 resin and subsequent purification of peptides by paper chroma...

Grinkevich, V.A.; Arzamazova, N.M.; Grinkevich-Kh, A.; Akimenko, Z.A.; Moroz, I.N.; Nazimov, I.V.; Aldanova, N.A., 1979: Primary structure of leucine iso leucine valine binding protein from escherichia coli 2. cyanogen bromide peptides. The splitting of carboxymethylated Leu, Ile, Val(LIV)-binding protein from E. coli by CNBr was performed. By gel-filtration, DEAE-chromatography and paper chromatography, 5 individual peptides out of 6 formed on cleavage were isolated. The arrange...

Ovchinnikov-Yu, A.; Aldanova, N.A.; Grinkevich, V.A.; Arzamazova, N.M.; Moroz, I.N.; Nazimov, I.V., 1977: The primary structure of leucine iso leucine valine binding protein from escherichia coli. The complete amino acid sequence of periplasmic protein from E. coli, selectively binding branched aliphatic amino acids such as leucine, isoleucine and valine (LIV-protein), was established. Exhaustive tryptic hydrolysis and splitting of the prot...

Saper, M.A.; Quiocho, F.A., 1983: Leucine iso leucine valine binding protein from escherichia coli structure at 3.0 angstrom resolution and location of the binding site. The structure of the leucine, isoleucine, valine-binding protein, an integral part of the high-affinity branched-chain aliphatic amino acid transport system in E. coli, was solved at 3.0-.ANG. resolution by X-ray crystallography. Five isomorphous...

Anonymous, 1979: Primary structure of liv binding protein from escherichia coli 1 peptides from exhaustive tryptic hydrolysis

Saper, M.A.; Quiocho, F.A., 1983: Leucine, isoleucine, valine-binding protein from Escherichia coli. Structure at 3.0-A resolution and location of the binding site. The structure of the leucine, isoleucine, valine-binding protein, an integral part of the high-affinity, branched-chain aliphatic amino acid transport system in Escherichia coli, has been solved at 3.0-A resolution by x-ray crystallography. Five i...

Nabiev I.; Trakhanov S.; Surin A.; Vorotyntseva T.; Efremov E.; Pletnev V., 1982: Optical spectroscopy study of substrate binding by leucine specific and leucine iso leucine valine binding proteins from escherichia coli. Voelter, W , Et Al (Ed ) Chemistry Of Peptides And Proteins, Vol 1; Proceedings Of The 3rd Ussr-Frg Symposium; Makachkala, Ussr, Oct 2-6, 1980 Xiii+554p Walter De Gruyter: Berlin, West Germany; New York, N Y , Usa Illus P467-472

Sack, J.S.; Saper, M.A.; Quiocho, F.A., 1989: Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. The three-dimensional structure of the native unliganded form of the Leu/Ile/Val-binding protein (Mr = 36,700), an essential component of the high-affinity active transport system for the branched aliphatic amino acids in Escherichia coli, has bee...

Williams W.L.S.; Freundlich M., 1969: Role of valine transfer rna in regulation of protein and rna synthesis in escherichia coli abstract iso leucine leucine enz valyl transfer rna synthetase valine starved cells. Bacteriological Proceedings 69: 51