On the biological significance of neurophysins: Presence of a major neurophysin in the sheep

Chauvet, M.T.; Coffe, Gérard; Chauvet, Jacqueline; Acher, Roger

doi:10.1016/0014-5793(75)80048-2

Cited by 14 publications

(9 citation statements)

References 12 publications

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“…The relative proportion of the major neurophysin, determined after separation by electrophoresis, is in agreement with that found in our crude neurophysin [8]. An amino acid sequence has been proposed for this neurophysin-111 by Schlesinger et al [24], simultaneously with our determination of the structure of MSEL-neurophysin [7].…”

Section: Alignment Of Tryp T Ic Pep Tidessupporting

confidence: 90%

“…hormone complexes by fractionated salt precipitation were carried out as described earlier [2,3]. Dissociation of the complexes by molecular sieving on Sephadex G-25 in 0.2 M acetic acid and chromatography of 'crude neurophysin' on DEAE-Sephadex A-50, were conducted as described in recent papers [8,9]. MSEL-neurophysins were eluted from DEAESephadex A-50 by a gradient of 0.2-0.4 M pyridine acetate buffer pH 5.9 (peak A).…”

Section: Purification Of Msel-neurophysinsmentioning

confidence: 99%

“…Table 1 gives the results obtained for 24, 48 and 72-h hydrolyses. The number of residues was calculated on the basis of six leucines per mole of protein which correspond to a molecular weight of approximately 10000 [8,9]. The molecule contains a single residue of methionine and a single residue of tyrosine.…”

Section: Partial Acid Hydrolysismentioning

confidence: 99%

“…At least two neurophysins, and perhaps three, exist in the posterior pituitary gland of the ox [31], the pig [32] and the sheep [8,23] as revealed by electrophoretic and sequential data. They have previously been called neurophysin I, I1 and 111 according to their electrophoretic mobilities [4].…”

Section: Comparison Between Msel-neurophysins and Vld V-neurophysinsmentioning

confidence: 99%

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The Neurohypophysial Hormone‐Binding Proteins: Complete Amino‐Acid Sequence of Ovine and Bovine MSEL‐Neurophysins

Chauvet

Acher

1976

European Journal of Biochemistry

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Ovine and bovine MSEL-neurophysins, purified by hormone protein complex precipitation, molecular sieving and ion-exchange chromatography, were subjected either to performic acid oxidation or to reduction and carboxamidomethylation. Cleavage by trypsin gave in each case eight fragments which were separated by peptide mapping. They were sequenced either directly by Edman degradation or after sub-cleavage by subtilisin, chymotrypsin, thermolysin, pepsin or partial acid hydrolysis and characterization of the sub-peptides.Alignment of the tryptic fragments was determined by automated Edman degradation and by identification of overlapping peptides obtained after hydrolysis of the polypeptide chain by chymotrypsin, pepsin and subtilisin. Bovine tryptic peptides were arranged, in part, according to their homology with ovine peptides.Both ovine and bovine MSEL-neurophysins comprise 95 residues ; in both cases, a three-residue N-terminal truncated form can be detected. Ovine and bovine MSEL-neurophysins are nearly identical. Two positions are different: 48 (isoleucine in ovine and asparagine in bovine) and 89 which shows a microheterogeneity in the ox (isoleucine in ovine, isoleucine or valine in bovine). Porcine MSEL-neurophysin presents four differences when compared with ovine homologue (positions 48, 89, 90 and 92) and an apparent three-residue C-terminal deletion.MSEL-neurophysins form a protein family which appears to be evolutionary stable in specieb of Artiodactyla. In this order of mammals, the rare variations seem to occur in the C-terminal sequence A second family of related neurophysins found in mammals, VLDV-neurophysins, shows substitutions in the N-terminal sequence when compared to MSEL-neurophysins. There is a large invariant central part in the polypeptide chain which might include the neurophysial hormone-binding domain of all neurophysins.

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Section: Alignment Of Tryp T Ic Pep Tidessupporting

confidence: 90%

Section: Purification Of Msel-neurophysinsmentioning

confidence: 99%

Section: Partial Acid Hydrolysismentioning

confidence: 99%

Section: Comparison Between Msel-neurophysins and Vld V-neurophysinsmentioning

confidence: 99%

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The Neurohypophysial Hormone‐Binding Proteins: Complete Amino‐Acid Sequence of Ovine and Bovine MSEL‐Neurophysins

Chauvet

Acher

1976

European Journal of Biochemistry

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“…Globular proteins are usually resistant to trypsin hydrolysis and only a few disulfide bridges can be reduced without urea. The great number of proline residues [7] can be partially responsible for the non-compact conformation of neurophysins. An analysis of the far-ultraviolet circular dichroism spectrum of bovine MSELneurophysin (Neurophysin-II) has suggested that this protein has 40% /I-structure and about 5% a-helix [3].…”

Section: Discussionmentioning

confidence: 99%