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J Meienhofer

Publications and source records attributed to J Meienhofer.

At least 55 records · Page 3Linked to original sources
PubMed1972

Primary structure of neocarzinostatin, an antitumor protein.

The antitumor protein neocarzinostatin is an acidic single-chain molecule, cross-linked by two disulfide bridges, and consists of 109 amino acid residues. Complete disulfide bond reduction and S-carboxymethylation was achieved in liquid ammonia. Sequence determination of five tryptic fragments led to the proposed primary structure.

Amino Acid Sequence↗
PubMed1972

Conformation of lysine vasopressin: a comparison with oxytocin.

Starting with assignments of proton nuclear magnetic resonance previously made for oxytocin in deuterated dimethylsulfoxide at 220 MHz, we have assigned resonances for the mammalian antidiuretic hormone, lysine vasopressin. The results demonstrate that spectral assignments of neurohypophyseal hormones and their congeners can, within certain limits, be derived from each other. Comparison of the spectra of lysine vasopressin and oxytocin suggests that the gross backbone conformations of their 20-membered ring components are for the most part similar in deuterated dimethylsulfoxide, whereas the C-terminal acyclic amino-acid sequence of lysine vasopressin is more flexible than that of oxytocin.

Deuterium↗
PubMed1971

Solid-phase synthesis with attachment of peptide to resin through an amino acid side chain: (8-lysine)-vasopressin.

It is proposed that the scope of solid-phase peptide synthesis could be considerably broadened by attaching peptides to the solid-phase through functional side-chain groups rather than through the commonly used alpha-carboxyl groups. Side-chain attachment offers the use of a large variety of chemical linkages to solid supports. Attachment through the epsilon-amino group of the lysine residue to a polystyrene resin has been applied to a solid-phase synthesis of lysine-vasopressin. N(alpha)-tert-butyl-oxycarbonyl-L-lysyl-glycinamide was condensed with chloroformoxymethyl polystyrene-2% divinylbenzene resin. After removal of the N(alpha)-protecting tert-butyloxycarbonyl group, the peptide chain was elongated by standard Merrifield procedures to give Tos-Cys(Bzl)-Tyr-Phe-Glu-(NH(2)) - Asp(NH(2)) - Cys(Bzl) - Pro - Lys(Z - resin) - Gly-NH(2). Cleavage from the resin with HBr in dioxane or trifluoroacetic acid gave a partially protected nonapeptide hydrobromide. For purification, it was converted into a fully protected peptide by treatment with benzyl p-nitro-phenyl carbonate and crystallized. Deprotection by sodium in liquid ammonia, oxidative cyclization, IRC-50 desalting, and ion-exchange chromatography gave lysinevasopressin with high potency in a rat-pressor assay.

Amino Acids↗