alpha-chymotrypsin and litorin

alpha-chymotrypsin has been researched along with litorin* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and litorin

Article	Year
Rohdei-litorin: a new peptide from the skin of Phyllomedusa rohdei. FEBS letters, 1985, Mar-11, Volume: 182, Issue:1 The bombesin-litorin family of peptides is characterized by the common amino acid sequence-Gly-His-X-Met-NH2 at the C-terminus, where X is a hydrophobic or aromatic residue. A new member of this family, rohdei-litorin, has been isolated from amphibian skin and its structure shown to be: Glp-Leu-Trp-Ala-Thr-Gly-His-Phe-Met-NH2. This new peptide displayed a greater affinity than other members of the family for rat urinary bladder receptors. A litorin-like peptide, with high affinity for this kind of receptor, has already been described in mammalian spinal cord and named neuromedin B. Rohdei-litorin shares with neuromedin B the entire C-terminal octrapeptide and may be considered the amphibian counterpart of this mammalian neuropeptide. Topics: Amino Acid Sequence; Amino Acids; Animals; Anura; Biological Assay; Chromatography, High Pressure Liquid; Chymotrypsin; Female; Gallbladder; Intestine, Large; Mammals; Oligopeptides; Pyrrolidonecarboxylic Acid; Skin; Urinary Bladder; Uterus	1985
Aminoacid composition and sequence of litorin, a bombesin-like nonapeptide from the skin of the Australian leptodactylid frog Litoria aurea. Experientia, 1975, May-15, Volume: 31, Issue:5 Topics: Amino Acid Sequence; Amino Acids; Animals; Anura; Bombesin; Carboxypeptidases; Chymotrypsin; Oligopeptides; Peptides; Skin	1975

Article

Year

Rohdei-litorin: a new peptide from the skin of Phyllomedusa rohdei.

FEBS letters, 1985, Mar-11, Volume: 182, Issue:1

The bombesin-litorin family of peptides is characterized by the common amino acid sequence-Gly-His-X-Met-NH2 at the C-terminus, where X is a hydrophobic or aromatic residue. A new member of this family, rohdei-litorin, has been isolated from amphibian skin and its structure shown to be: Glp-Leu-Trp-Ala-Thr-Gly-His-Phe-Met-NH2. This new peptide displayed a greater affinity than other members of the family for rat urinary bladder receptors. A litorin-like peptide, with high affinity for this kind of receptor, has already been described in mammalian spinal cord and named neuromedin B. Rohdei-litorin shares with neuromedin B the entire C-terminal octrapeptide and may be considered the amphibian counterpart of this mammalian neuropeptide.

Topics: Amino Acid Sequence; Amino Acids; Animals; Anura; Biological Assay; Chromatography, High Pressure Liquid; Chymotrypsin; Female; Gallbladder; Intestine, Large; Mammals; Oligopeptides; Pyrrolidonecarboxylic Acid; Skin; Urinary Bladder; Uterus

1985

Aminoacid composition and sequence of litorin, a bombesin-like nonapeptide from the skin of the Australian leptodactylid frog Litoria aurea.

Experientia, 1975, May-15, Volume: 31, Issue:5

Topics: Amino Acid Sequence; Amino Acids; Animals; Anura; Bombesin; Carboxypeptidases; Chymotrypsin; Oligopeptides; Peptides; Skin

1975