A new family of growth factor-like peptides 'Trefoil' disulphide loop structures as a common feature in breast cancer associated peptide (pS2), pancreatic spasmolytic polypeptide (PSP), and frog skin peptides (spasmolysins)

FEBS Letters

Volumn 250, Issue 1, 1989, Pages 85-90

  Thim, Lars ^a  

^a Novo Research Institute   (Denmark)

Author keywords

Amino acid sequence comparison; Disulfide bond; Domain structure; Receptor binding

Indexed keywords

GROWTH FACTOR; PROXYPHYLLINE;

BREAST CANCER; CANCER ASSOCIATED PROTEIN; HUMAN; NONHUMAN; PANCREAS SPASMOLYTIC POLYPEPTIDE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN STRUCTURE; REVIEW; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMAL; BREAST NEOPLASMS; CELL LINE; COMPARATIVE STUDY; FEMALE; GASTRIC JUICE; GROWTH SUBSTANCES; HUMAN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PARASYMPATHOLYTICS; PEPTIDES; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, NUCLEIC ACID; XENOPUS LAEVIS;

EID: 0024349761     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(89)80690-8     Document Type: Article

References (38)

1. Pancreatic Spasmolytic Polypeptide (PSP): I. Preparation and initial chemical characterization of a new polypeptide from porcine pancreas
2. Pancreatic Spasmolytic Polypeptide (PSP): III. Pharmacology of a new porcine pancreatic polypeptide with spasmolytic and gastric acid secretion inhibitory effects