Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments

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Standard

Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments. / Rasmussen, T N; Bersani, M; Johnsen, A H; Kofod, Hans; Holst, J J.

In: Peptides, Vol. 15, No. 1, 1994, p. 89-94.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rasmussen, TN, Bersani, M, Johnsen, AH, Kofod, H & Holst, JJ 1994, 'Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments', Peptides, vol. 15, no. 1, pp. 89-94.

APA

Rasmussen, T. N., Bersani, M., Johnsen, A. H., Kofod, H., & Holst, J. J. (1994). Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments. Peptides, 15(1), 89-94.

Vancouver

Rasmussen TN, Bersani M, Johnsen AH, Kofod H, Holst JJ. Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments. Peptides. 1994;15(1):89-94.

Author

Rasmussen, T N ; Bersani, M ; Johnsen, A H ; Kofod, Hans ; Holst, J J. / Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments. In: Peptides. 1994 ; Vol. 15, No. 1. pp. 89-94.

Bibtex

@article{66c58fb074ce11dbbee902004c4f4f50,
title = "Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments",
abstract = "Using radioimmunoassays with two different antisera, one directed towards the C-terminal and one towards the mid part of porcine and human alpha-CGRP, respectively, we isolated three immunoreactive peptides from acid/ethanol extracts of porcine spinal cord by means of HPLC. By amino acid sequence analysis and mass spectrometry (PDMS), the most abundant peptide was found to be identical to the 37 residue CGRP previously isolated from porcine adrenal glands and spinal cord. The two remaining peptides were identified as pCGRP(18-37) and pCGRP(19-37). Furthermore, the oxidized forms (oxidized Met in position 22) of all three peptides were isolated. We extracted a large amount of tissue and the extractable peptides were purified without discarding side fractions. The purification steps were monitored by immunochemical methods that are highly sensitive for human alpha- and beta-CGRP. Yet we were unable to detect any second full-length form of CGRP. Thus, we conclude that only a single form of full-length CGRP is found in pigs and that this peptide may be cleaved to produce potentially bioactive N- and C-terminal fragments.",
keywords = "Amino Acid Sequence, Animals, Calcitonin Gene-Related Peptide, Mass Spectrometry, Molecular Sequence Data, Peptide Fragments, Radioimmunoassay, Swine",
author = "Rasmussen, {T N} and M Bersani and Johnsen, {A H} and Hans Kofod and Holst, {J J}",
year = "1994",
language = "English",
volume = "15",
pages = "89--94",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments

AU - Rasmussen, T N

AU - Bersani, M

AU - Johnsen, A H

AU - Kofod, Hans

AU - Holst, J J

PY - 1994

Y1 - 1994

N2 - Using radioimmunoassays with two different antisera, one directed towards the C-terminal and one towards the mid part of porcine and human alpha-CGRP, respectively, we isolated three immunoreactive peptides from acid/ethanol extracts of porcine spinal cord by means of HPLC. By amino acid sequence analysis and mass spectrometry (PDMS), the most abundant peptide was found to be identical to the 37 residue CGRP previously isolated from porcine adrenal glands and spinal cord. The two remaining peptides were identified as pCGRP(18-37) and pCGRP(19-37). Furthermore, the oxidized forms (oxidized Met in position 22) of all three peptides were isolated. We extracted a large amount of tissue and the extractable peptides were purified without discarding side fractions. The purification steps were monitored by immunochemical methods that are highly sensitive for human alpha- and beta-CGRP. Yet we were unable to detect any second full-length form of CGRP. Thus, we conclude that only a single form of full-length CGRP is found in pigs and that this peptide may be cleaved to produce potentially bioactive N- and C-terminal fragments.

AB - Using radioimmunoassays with two different antisera, one directed towards the C-terminal and one towards the mid part of porcine and human alpha-CGRP, respectively, we isolated three immunoreactive peptides from acid/ethanol extracts of porcine spinal cord by means of HPLC. By amino acid sequence analysis and mass spectrometry (PDMS), the most abundant peptide was found to be identical to the 37 residue CGRP previously isolated from porcine adrenal glands and spinal cord. The two remaining peptides were identified as pCGRP(18-37) and pCGRP(19-37). Furthermore, the oxidized forms (oxidized Met in position 22) of all three peptides were isolated. We extracted a large amount of tissue and the extractable peptides were purified without discarding side fractions. The purification steps were monitored by immunochemical methods that are highly sensitive for human alpha- and beta-CGRP. Yet we were unable to detect any second full-length form of CGRP. Thus, we conclude that only a single form of full-length CGRP is found in pigs and that this peptide may be cleaved to produce potentially bioactive N- and C-terminal fragments.

KW - Amino Acid Sequence

KW - Animals

KW - Calcitonin Gene-Related Peptide

KW - Mass Spectrometry

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Radioimmunoassay

KW - Swine

M3 - Journal article

C2 - 8015985

VL - 15

SP - 89

EP - 94

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 1

ER -

ID: 262119