Reduced behavioral effectiveness of ACTH(1-24) after a second administration: interaction with opiates.

Repeated intraventricular administration of ACHT results in reduction of subsequent ACTH-induced grooming behavior. A previous injection of beta-endorphin, (D-Phe(7))ACTH(4-10), or morphine, also reduces the behavioral response to a subsequent injection of ACTH. The reduction in grooming as a result of repeated administration is not mediated by corticosteroid feedback and can be eliminated by pretreatment with the opiate antagonist naloxone.

Molecular data on urinary glycoproteins with human leucocyte antigen (HLA) activity.

Two glycoproteins characterized by their serological activities (HLA-A9 and HLA-B12), their isoelectric points and their molecular weights were purified from urine from a patient suffering from tubular proteinuria (cystinosis). Their physicochemical properties as well as an important increase of their specific activities during the different purification steps suggested that they behave as human leucocyte antigens (HLA) which had been excreted into urine. Their amino acid compositions and N-terminal sequences were different to those described for HLA solubilized from cultured human lymphoblast cell lines.

[Molecular aspects of 2 human urinary glycoproteins with histocompatibility antigen (HLA) serological activity].

Two serologically active urinary glycoproteins (HLA-A 9 and HLA-B 12) were isolated from urine provided by a patient suffering from tubular proteinuria. Their N-terminal sequences were automatically determined. The latter were identical with the sequence of another urinary glycoprotein (protein HC).

The ostrich (Struthio camelus) egg-white lysozyme.

The purification of Ostrich (Struthio camelus) egg-white lysozyme is reported. The quantitative amino acid composition, the molecular weight, the N-terminal sequence (34 amino acids) as well as kinetic studies allow to range this enzyme among the goose type lysozymes.

The evolution of gonadotropins: some molecular data concerning a non-mammalian pituitary gonadotropin, the hormone from a teleost fish (Cyprinus carpio L.).

The amino acid and sugar compositions as well as long N-terminal sequences and the C-terminal amino acids of the two subunits of carp gonadotropin, SU I and SU II, were determined. An important homology was demonstrated between SU I and alpha-subunits and between SU II and beta-subunits of mammalian gonadotropins. Moreover SU II was more closely related to the beta-subunit of LH than to the beta-subunit of FSH.

Amino acid sequence and immunological properties of chalchalaca egg white lysozyme.

The amino acid sequence of lysozyme c from chachalaca egg white was determined. Like other bird lysozymes c, that of the chachalaca has 129 amino acid residues. It differs from other avian lysozymes c by 2 to 31 amino acid substitutions as well as by being devoid of phenylalanine.

Study of the apoprotein of Folch-Pi bovine proteolipid. II. Characterization of the components isolated from sodium dodecyl sulfate solutions.

Acrylamide gel electrophoresis in dodecyl sulfate solutions of Folch-Pi apoprotein shows several bands. The different components were separated by Biogel P-200 filtration and then reduced and carboxymethylated. A comparative study of the amino acid composition, N-terminal sequence and C-terminal amino acid of the different components led to the assumption that their primary sequences are similar.

The losozyme from Asterias rubens.

Lysozyme (mucopeptide N-acetylmuramylhydrolase) from Asterias rubens was obtained in a chromatographically and electrophoretically pure state by gel filtration and affinity chromatography. The quantitative amino acid composition, the molecular weight and the N-terminal sequence determined by a sequencer are reported. This new invertebrate enzyme presents important differences when compared to previously studied lysozymes.