BIOMAT Database Logo BIOMAT Database Logo

Evidence for higher molecular weight immunoreactive forms of vasopressin in the mouse hypothalamus. Relationships with putative proneurophysins. 1979

M Camier, and M Lauber, and J Möhring, and P Cohen

UI MeSH Term Description Entries
D007031 Hypothalamus Ventral part of the DIENCEPHALON extending from the region of the OPTIC CHIASM to the caudal border of the MAMMILLARY BODIES and forming the inferior and lateral walls of the THIRD VENTRICLE. Lamina Terminalis,Preoptico-Hypothalamic Area,Area, Preoptico-Hypothalamic,Areas, Preoptico-Hypothalamic,Preoptico Hypothalamic Area,Preoptico-Hypothalamic Areas
D007118 Immunoassay A technique using antibodies for identifying or quantifying a substance. Usually the substance being studied serves as antigen both in antibody production and in measurement of antibody by the test substance. Immunochromatographic Assay,Assay, Immunochromatographic,Assays, Immunochromatographic,Immunoassays,Immunochromatographic Assays
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009481 Neurophysins Carrier proteins for OXYTOCIN and VASOPRESSIN. They are polypeptides of about 10-kDa, synthesized in the HYPOTHALAMUS. Neurophysin I is associated with oxytocin and neurophysin II is associated with vasopressin in their respective precursors and during transportation down the axons to the neurohypophysis (PITUITARY GLAND, POSTERIOR). Neurophysin,Neurophysin I,Neurophysin II,Neurophysin III,Oxytocin-Associated Neurophysin,Vasopressin-Associated Neurophysin,Neurophysin, Oxytocin-Associated,Neurophysin, Vasopressin-Associated,Oxytocin Associated Neurophysin,Vasopressin Associated Neurophysin
D011498 Protein Precursors Precursors, Protein
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014667 Vasopressins Antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (structure varies with species) to regulate water balance and OSMOLARITY. In general, vasopressin is a nonapeptide consisting of a six-amino-acid ring with a cysteine 1 to cysteine 6 disulfide bridge or an octapeptide containing a CYSTINE. All mammals have arginine vasopressin except the pig with a lysine at position 8. Vasopressin, a vasoconstrictor, acts on the KIDNEY COLLECTING DUCTS to increase water reabsorption, increase blood volume and blood pressure. Antidiuretic Hormone,Antidiuretic Hormones,beta-Hypophamine,Pitressin,Vasopressin,Vasopressin (USP),Hormone, Antidiuretic,beta Hypophamine
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus

Related Publications

M Camier, and M Lauber, and J Möhring, and P Cohen
Evidence for high molecular weight immunoreactive thyrotropin-releasing hormone (TRH) precursor forms in the developing mouse hypothalamus. Simultaneous immunolocalization with TRH in cultured neurons.
May 1990, Endocrinology,
M Camier, and M Lauber, and J Möhring, and P Cohen
Ontogeny and molecular weight of immunoreactive arginine vasopressin and corticotropin-releasing factor in the ovine fetal hypothalamus.
January 1996, Peptides,
M Camier, and M Lauber, and J Möhring, and P Cohen
Intestinal and pancreatic glucagon-like peptides. Evidence for identity of higher molecular weight forms.
April 1979, The Journal of biological chemistry,
M Camier, and M Lauber, and J Möhring, and P Cohen
Molecular-weight profiles of immunoreactive corticotropin in the hypothalamus of the aging rat.
January 1982, Brain research,
M Camier, and M Lauber, and J Möhring, and P Cohen
Galanin immunoreactive neurons in the human hypothalamus: colocalization with vasopressin-containing neurons.
August 1990, The Journal of comparative neurology,
M Camier, and M Lauber, and J Möhring, and P Cohen
Somatostatin immunoreactive peptides of higher molecular weight in ovine hypothalamic extracts.
June 1978, The Journal of endocrinology,
M Camier, and M Lauber, and J Möhring, and P Cohen
Vasopressin- and oxytocin-immunoreactive nerve cells in the aging rat hypothalamus.
January 1996, Acta physiologica et pharmacologica Bulgarica,
M Camier, and M Lauber, and J Möhring, and P Cohen
In vitro characterization of the Mig1 repressor from Saccharomyces cerevisiae reveals evidence for monomeric and higher molecular weight forms.
December 2006, Yeast (Chichester, England),
M Camier, and M Lauber, and J Möhring, and P Cohen
Multiple molecular weight forms of immunoreactive alpha-inhibin in human seminal plasma.
February 1993, The Journal of clinical endocrinology and metabolism,
M Camier, and M Lauber, and J Möhring, and P Cohen
Molecular forms of immunoreactive gonadotropin-releasing hormone in hypothalamus and testis of the frog, Rana esculenta.
September 1989, General and comparative endocrinology,
Copied contents to your clipboard!