Publication | Closed Access
ISOLATION, PURIFICATION, AND CHARACTERIZATION OF γ-LIPOTROPIC HORMONE FROM SHEEP PITUITARY GLANDS
195
Citations
16
References
1967
Year
Human GrowthSheep Pituitary GlandsPeptide SciencePeptide TherapeuticsAdipokinesGastrointestinal Peptide HormonePituitary GlandActive PolypeptideHypothalamic PeptidePituitary DiseasePublic HealthAnimal PhysiologyBiochemistryEndocrine MechanismMedicineEndocrinologyAnimal SciencePhysiologyReceptor BiologyPituitary Peptide BiosynthesisEndocrine Research
The isolation and characterization of a new biologically active polypeptide from sheep pituitary glands is described. Considerable evidence suggests that the structure of the new molecule, designated γ-lipotropin, is identical with the N-terminal portion (sequence 1–58) of β-lipotropin and, therefore, that γ-lipotropin contains at its C-terminus the amino acid sequence of β-melanophore-stirnulating hormone (β-MSH). The implications of these results are discussed in relation to the mechanism of pituitary peptide biosynthesis and to the structure–activity relationships between sheep β-MSH and lipotropic hormones.
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