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Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

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Standard

Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones. / Nothacker, H P; Rinehart, K L; Grimmelikhuijzen, C J.

I: Biochemical and Biophysical Research Communications, Bind 179, Nr. 3, 30.09.1991, s. 1205-11.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Nothacker, HP, Rinehart, KL & Grimmelikhuijzen, CJ 1991, 'Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones', Biochemical and Biophysical Research Communications, bind 179, nr. 3, s. 1205-11.

APA

Nothacker, H. P., Rinehart, K. L., & Grimmelikhuijzen, C. J. (1991). Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones. Biochemical and Biophysical Research Communications, 179(3), 1205-11.

Vancouver

Nothacker HP, Rinehart KL, Grimmelikhuijzen CJ. Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones. Biochemical and Biophysical Research Communications. 1991 sep 30;179(3):1205-11.

Author

Nothacker, H P ; Rinehart, K L ; Grimmelikhuijzen, C J. / Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones. I: Biochemical and Biophysical Research Communications. 1991 ; Bind 179, Nr. 3. s. 1205-11.

Bibtex

@article{99581cf7498c454996ced8a2f1369fd4,
title = "Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones",
abstract = "We have isolated and sequenced the neuropeptide L-3-phenyllactyl-Phe-Lys-Ala-NH2 from the sea anemone Anthopleura elegantissima. This neuropeptide (named Antho-KAamide) has the unusual N-terminal L-3-phenyllactyl blocking group which has recently also been discovered in 2 other neuropeptides from sea anemones. We propose that the L-3-phenyllactyl residue renders Antho-KAamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the neuropeptide after neuronal release. The existence of the L-3-phenyllactyl residue in 3 neuropeptides isolated so far suggests that this blocking group is more generally occurring.",
keywords = "Amino Acid Sequence, Animals, Cnidaria, Immunohistochemistry, Molecular Sequence Data, Neuropeptides, Radioimmunoassay, Sea Anemones, Sequence Homology, Nucleic Acid, Spectrometry, Mass, Fast Atom Bombardment",
author = "Nothacker, {H P} and Rinehart, {K L} and Grimmelikhuijzen, {C J}",
year = "1991",
month = sep,
day = "30",
language = "English",
volume = "179",
pages = "1205--11",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

AU - Nothacker, H P

AU - Rinehart, K L

AU - Grimmelikhuijzen, C J

PY - 1991/9/30

Y1 - 1991/9/30

N2 - We have isolated and sequenced the neuropeptide L-3-phenyllactyl-Phe-Lys-Ala-NH2 from the sea anemone Anthopleura elegantissima. This neuropeptide (named Antho-KAamide) has the unusual N-terminal L-3-phenyllactyl blocking group which has recently also been discovered in 2 other neuropeptides from sea anemones. We propose that the L-3-phenyllactyl residue renders Antho-KAamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the neuropeptide after neuronal release. The existence of the L-3-phenyllactyl residue in 3 neuropeptides isolated so far suggests that this blocking group is more generally occurring.

AB - We have isolated and sequenced the neuropeptide L-3-phenyllactyl-Phe-Lys-Ala-NH2 from the sea anemone Anthopleura elegantissima. This neuropeptide (named Antho-KAamide) has the unusual N-terminal L-3-phenyllactyl blocking group which has recently also been discovered in 2 other neuropeptides from sea anemones. We propose that the L-3-phenyllactyl residue renders Antho-KAamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the neuropeptide after neuronal release. The existence of the L-3-phenyllactyl residue in 3 neuropeptides isolated so far suggests that this blocking group is more generally occurring.

KW - Amino Acid Sequence

KW - Animals

KW - Cnidaria

KW - Immunohistochemistry

KW - Molecular Sequence Data

KW - Neuropeptides

KW - Radioimmunoassay

KW - Sea Anemones

KW - Sequence Homology, Nucleic Acid

KW - Spectrometry, Mass, Fast Atom Bombardment

M3 - Journal article

C2 - 1681803

VL - 179

SP - 1205

EP - 1211

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

ID: 33514215