Valosin: isolation and characterization of a novel peptide from porcine intestine

Wolfgang E. Schmidt; Viktor Mutt; Mats Carlquist; Hartmut Kratzin; J. Michael Conlon; Werner Creutzfeldt

doi:10.1016/0014-5793(85)80021-1

Valosin: isolation and characterization of a novel peptide from porcine intestine

Wolfgang E. Schmidt, Viktor Mutt, Mats Carlquist, Hartmut Kratzin, J. Michael Conlon, Werner Creutzfeldt

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

The isolation and primary structure of a novel gastrointestinal peptide, designated valosin, is described. The peptide was purified from porcine upper gut extracts using an HPLC and N-terminal sequence screening strategy which depends on Chromatographic and structural characteristics as isolation criterion. The amino acid sequence of this peptide consists of 25 amino acid residues: V Q Y P V E H P D K F L K F G M T P S K G V L F Y. It does not show structural homology to known protein or nucleotide sequences. According to preliminary experiments, valosin possesses biological effects on the gastrointestinal tract of the dog.

Original language	English
Pages (from-to)	264-268
Number of pages	5
Journal	FEBS Letters
Volume	191
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(85)80021-1
Publication status	Published (in print/issue) - 28 Oct 1985

Keywords

Gastrointestinal peptide
HPLC-sequence screening Primary structure
Isolation
Porcine gut extract
Valosin

Access to Document

10.1016/0014-5793(85)80021-1

Cite this

@article{c43c10b3f33b4546b55365747141afb1,

title = "Valosin: isolation and characterization of a novel peptide from porcine intestine",

abstract = "The isolation and primary structure of a novel gastrointestinal peptide, designated valosin, is described. The peptide was purified from porcine upper gut extracts using an HPLC and N-terminal sequence screening strategy which depends on Chromatographic and structural characteristics as isolation criterion. The amino acid sequence of this peptide consists of 25 amino acid residues: V Q Y P V E H P D K F L K F G M T P S K G V L F Y. It does not show structural homology to known protein or nucleotide sequences. According to preliminary experiments, valosin possesses biological effects on the gastrointestinal tract of the dog.",

keywords = "Gastrointestinal peptide, HPLC-sequence screening Primary structure, Isolation, Porcine gut extract, Valosin",

author = "Schmidt, {Wolfgang E.} and Viktor Mutt and Mats Carlquist and Hartmut Kratzin and Conlon, {J. Michael} and Werner Creutzfeldt",

year = "1985",

month = oct,

day = "28",

doi = "10.1016/0014-5793(85)80021-1",

language = "English",

volume = "191",

pages = "264--268",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons, Inc.",

number = "2",

}

TY - JOUR

T1 - Valosin

T2 - isolation and characterization of a novel peptide from porcine intestine

AU - Schmidt, Wolfgang E.

AU - Mutt, Viktor

AU - Carlquist, Mats

AU - Kratzin, Hartmut

AU - Conlon, J. Michael

AU - Creutzfeldt, Werner

PY - 1985/10/28

Y1 - 1985/10/28

N2 - The isolation and primary structure of a novel gastrointestinal peptide, designated valosin, is described. The peptide was purified from porcine upper gut extracts using an HPLC and N-terminal sequence screening strategy which depends on Chromatographic and structural characteristics as isolation criterion. The amino acid sequence of this peptide consists of 25 amino acid residues: V Q Y P V E H P D K F L K F G M T P S K G V L F Y. It does not show structural homology to known protein or nucleotide sequences. According to preliminary experiments, valosin possesses biological effects on the gastrointestinal tract of the dog.

AB - The isolation and primary structure of a novel gastrointestinal peptide, designated valosin, is described. The peptide was purified from porcine upper gut extracts using an HPLC and N-terminal sequence screening strategy which depends on Chromatographic and structural characteristics as isolation criterion. The amino acid sequence of this peptide consists of 25 amino acid residues: V Q Y P V E H P D K F L K F G M T P S K G V L F Y. It does not show structural homology to known protein or nucleotide sequences. According to preliminary experiments, valosin possesses biological effects on the gastrointestinal tract of the dog.

KW - Gastrointestinal peptide

KW - HPLC-sequence screening Primary structure

KW - Isolation

KW - Porcine gut extract

KW - Valosin

UR - http://www.scopus.com/inward/record.url?scp=0022375050&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(85)80021-1

DO - 10.1016/0014-5793(85)80021-1

M3 - Article

C2 - 4054310

AN - SCOPUS:0022375050

SN - 0014-5793

VL - 191

SP - 264

EP - 268

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Valosin: isolation and characterization of a novel peptide from porcine intestine

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this