W.B. Watkins

University of Auckland

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V.J. Choy

Health Research Council of New Zealand

L. G. Moore

AgResearch

C.W. Small

Lunenfeld-Tanenbaum Research Institute

A. J. Peterson

Lawrence Livermore National Laboratory

R. J. Fairclough

Ministry for Primary Industries

John C. Peek

Erasmus University Rotterdam

H.R. Tervit

Cawthron Institute

H. K. ELLIS

University of Auckland

R. Bock

Hertfordshire Community NHS Trust

John J. Evans

University of Otago

Cooperative Institutions

University of Auckland

University of California, San Diego

Salk Institute for Biological Studies

AgResearch

United States Department of Veterans Affairs

Ministry for Primary Industries

The University of Texas Health Science Center at San Antonio

The University of Texas Health Science Center at Houston

University of Otago

University of Florida

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Precautions in the application of immunohistochemical techniques to tissues of the pig hypothalamo-neurohypophysial system.

Journal of Histochemistry & Cytochemistry (1977)

W.B. Watkins

Immunohistochemical procedures were used to localize neurophysin in the hypothalamo-neurohypophysial axis of the domestic pig. The topographical distribution of neurophysin as revealed by the immunofluorescence "sandwich" technique was similar to that found when either the immunoglobulin-peroxidase bridge method or the peroxidase-labeled gamma-globulin technique was employed. However, application of the peroxidase-anti-peroxidase (PAP) complex procedure resulted in nonspecific staining of the magnocellular structures. This phenomenon was attributed to the action of PAP on the tissue and after screening a number of other vertebrate species was found to be unique to the pig. Minimal nonspecific binding of the PAP could be achieved either by reducing the reaction time of PAP to 5 min or, by the addition of 1% (v/v) normal serum to all reagents and wash solution. That the PAP-binding protein is a component of the hypothalamo-neurohypophysial axons is discussed.

Neurophysins

Immunofluorescence

10.1177/25.1.319165

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Citations (12)

DEMONSTRATION BY IMMUNOPEROXIDASE HISTOCHEMISTRY OF CALCITONIN IN THE ANTERIOR LOBE OF THE RAT PITUITARY

The Journal of Clinical Endocrinology & Metabolism (1978)

Leonard J. Deftos D. W. Burton Bayard D. Catherwood Henry G. Bone Jacqueline G. Parthemore

We have demonstrated by a specific immunoperoxidase procedure the presence of calcitonin-containing cells in the rat pituitary gland. These cells are widely distributed throughout the anterior lobe and seem to constitute the entire population of cells of the intermediate lobe. No such cells were seen in the posterior lobe. The presence of calcitonin-containing cells in the pituitary provides novel implications about the physiological significance of this hormone.

Immunoperoxidase

Lobe

Posterior pituitary

10.1210/jcem-47-2-457

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Citations (117)

DISTRIBUTION OF SOLUBLE PROTEINS IN THE MAMMALIAN NEUROHYPOPHYSIS AND THEIR CROSS-SPECIES REACTIVITY WITH ANTI-NEUROPHYSIN

Journal of Endocrinology (1972)

H. K. ELLIS W.B. Watkins John J. Evans

SUMMARY Pituitary glands were collected from a selection of 22 domestic and exotic mammalian species. The soluble proteins extracted from the neurohypophyses were characterized by horizontal starch-gel electrophoresis at pH 8·1. Those species which were closely related phylogenetically, e.g. fallow deer and muntjac deer, pig and hippopotamus, dog and coatimundi, and members of the primates, had similar and in some cases identical protein profiles. The ability of proteins extracted from the starch-gel to cross-react immunologically with an antiserum raised against porcine neurophysin-II was determined by microimmunodiffusion. Using this technique for the identification of neurophysins in conjunction with osmotic stimulation experiments, it was found that the number of major neurophysins present in the mammalian neurohypophyses studied varied from one in the guinea-pig and hedgehog to four in man. The concept of multiple neurophysins is discussed.

Neurophysins

10.1677/joe.0.0550565

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Citations (18)

NEUROPHYSINS OF THE RAT

Journal of Endocrinology (1972)

W.B. Watkins

Three neurophysins have been isolated and biochemically characterized from the ox (Rauch, Hollenberg & Hope, 1969), pig (Uttenthal & Hope, 1970) and sheep (Watkins, 1972) while the presence of a neurophysin has been demonstrated in cod pituitary glands (Pickering, 1968). By means of immunological and biosynthesis techniques, Norstrom, Sjöstrand, Livett, Uttenthal & Hope, (1971) have tentatively identified one neurophysin in the rat posterior pituitary gland. In a recent extension of this work, Burford, Jones & Pickering (1971) using polyacrylamide electrophoresis have been able to resolve the major rat posterior pituitary gland protein into two major components one of which was tentatively described as an oxytocin-neurophysin and the other as a vasopressin—neurophysin. In this present investigation, the neurophysins of the rat were fractionated using procedures previously established for the purification of the ox, pig and sheep neurophysins. The protein-hormone complex was prepared in a yield of 26·9 mg from an

Neurophysins

Posterior pituitary

10.1677/joe.0.0530331

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Citations (3)

NEUROPHYSINS OF THE HUMAN PITUITARY GLAND

Journal of Endocrinology (1971)

W.B. Watkins

The polypeptide hormones of the posterior pituitary gland, oxytocin and vasopressin, can be precipitated out of solution by the addition of sodium chloride to an extract of the gland. The hormones are salted-out complexed to the soluble proteins known as neurophysins and this protein-hormone complex has been found to possess the pressor and oxytocic activities in ratios similar to those found in the fresh gland (van Dyke, Chow, Greep & Rothen 1942). Neurophysins have been isolated from the pig (Uttenthal & Hope, 1970), ox (Rauch, Hollenberg & Hope, 1969) and cod (Pickering, 1968). In the present paper the proteins precipitated from the posterior lobe of the human pituitary gland were investigated by gel exclusion chromatography and starch gel electrophoresis, and their ability to bind oxytocin and vasopressin was determined. Acetone-dried posterior pituitary lobes (2·4 g) were extracted for 24 h at 4 °C in 0·1 m-hydrochloric acid (100 ml),

Neurophysins

Posterior pituitary

Endocrine gland

10.1677/joe.0.0510595

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Citations (15)

Chemistry of the podocarpaceae—XV

Tetrahedron (1968)

Brian R. Davis W.B. Watkins

Anisole

Derivative (finance)

Side chain

Diketene

10.1016/0040-4020(68)88118-9

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Citations (8)

Deamination of 19-norabieta-8,11,13-trien-4-amine

Tetrahedron Letters (1968)

R.N. Seelye W.B. Watkins

Deamination

Oxidative deamination

10.1016/s0040-4039(01)98934-8

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Citations (4)

A comparative study of partial neurophysin protein sequences of cod, guinea pig, rat and sheep

FEBS Letters (1977)

David H. Schlesinger B. T. Pickering W.B. Watkins J.C. Peek L. G. Moore

10.1016/0014-5793(77)80478-x

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Citations (15)

THE ISOLATION AND BIOCHEMICAL CHARACTERIZATION OF THREE NEUROPHYSINS OF THE SHEEP

Journal of Endocrinology (1973)

W.B. Watkins

SUMMARY Three neurophysins have been isolated from acetone-dried sheep posterior lobe powder and have been named neurophysins I, II and III. Neurophysins I, II and III account for approximately 15, 15 and 70%, respectively of the total neurohypophysial hormone-binding proteins present in the sheep posterior pituitary lobe. All the neurophysins bind oxytocin and [8-arginine]-vasopressin. Neurophysins I and II each were found to contain one molecule of histidine/molecule of protein but to lack methionine, whereas neurophysin III contained no histidine but had one molecule of methionine/molecule of protein. The molecular weights of sheep neurophysins I, II and III were 11348, 9803 and 10377, respectively, as determined by amino acid analysis. An approximate value of 10000 was estimated for the apparent molecular weight of the neurophysins by gel exclusion chromatography on Sephadex G-75. Solid amorphous complexes were formed between the neurophysins and oxytocin as well as with [8-arginine]-vasopressin. In each case one molecule of neurophysin complexed with one molecule of hormone. The stoichiometry of the sheep neurophysins relative to the neurohypophysial hormones is discussed.

Neurophysins

Posterior pituitary

Sephadex

10.1677/joe.0.0590017

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Citations (23)

A rapid and specific method for the determination of oxytocinase (cystine aminopeptidase) activity using continuous flow analysis and S-benzyl-L-cysteine-P-nitroanilide as substrate

Clinical Biochemistry (1975)

C.W. Small W.B. Watkins

Thiazolidine

10.1016/s0009-9120(75)91273-4

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Citations (3)