Results 111 to 120 of about 354,799 (167)
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The reaggregation of purified subunits of alpha-crystallin

Experimental Eye Research, 1973
Abstract Ultracentrifuge studies have been carried out with reaggregated macromolecules obtained from purified subunits of low MW calf lens alpha-crystallin. The subunits were isolated by affinity chromotography with para-amino-phenyl mercuric acetate-Agarose columns followed by chromatography with DEAE-cellulose in 7 m urea.
L K, Li, A, Spector
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II. Immunochemical studies on alpha crystallin subunits

Experimental Eye Research, 1972
Abstract Carboxymethylated alpha crystallin subunits yield a clearer separation of the acidic and basic subunit molecules than native alpha crystallin subunits. A minimum of four distinct subunit molecules could be observed in all fractionation procedures tested.
D, Zouzias, W, Manski
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Kinetics of oxygen binding and subunit assembly for the hemoglobin alpha subunit

Biophysical Chemistry, 1992
A thorough kinetic characterization of the O2-binding and self-association reactions of alpha-subunits of human hemoglobin A has been performed. All of the rate constants for a five step reaction model linking the monomer-dimer reaction to the O2-binding steps have been determined for the first time.
W T, Windsor   +3 more
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A monosaccharide is bound to the sodium-pump .alpha.-subunit

Biochemistry, 1992
We have recently reported that the Na pump alpha-subunit has cytosolic-oriented oligosaccharides which were sensitive to cleavage by an enzyme specific for hydrolysis of N-linked glycans [Pedemonte et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 9789-9793].
C H, Pedemonte, J H, Kaplan
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Detection of the alpha-subunit of inhibin in trophoblastic neoplasia

Human Pathology, 1999
Placental trophoblasts are the primary source of serum inhibin during pregnancy. We sought to characterize inhibin immunolabeling in trophoblastic neoplasms and compare the results with those for established markers of trophoblastic differentiation. Formalin-fixed, paraffin-embedded tissues from three normal term placentas, 13 hydatidiform moles (HM ...
T J, Pelkey   +3 more
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Structure of Human Luteinizing Hormone Alpha Subunit

Endocrine Research Communications, 1978
Structural studies have substantiated the concept that the glycoprotein hormones consist of a "common" alpha subunit and "hormone-specific" beta subunit. Despite this, consensus is still lacking concerning certain portions of the amino acid sequences, including alignment of residues 81--82 in the alpha subunit.
H T, Keutmann   +3 more
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Affinity of Stat2 for the Subunits of the Interferon Alpha Receptor

Biochemistry, 2002
The interferon alpha receptor is composed of two subunits: IFNaR1 and IFNaR2. Interferon alpha binding to the receptor induces phosphorylation of tyrosine 466 on IFNaR1, which in turn binds the SH2 domain of the latent transcription factor Stat2 to initiate signaling. Stat2 also binds to IFNaR2 in a constitutive, phosphorylation-independent manner.
Abu Z M, Saleh   +2 more
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Pure alpha subunit-secreting pituitary tumors

Journal of Neurosurgery, 1983
✓ The authors describe six patients with pituitary macroadenomas hypersecreting only the alpha subunit of the glycoprotein hormones. These patients had been previously diagnosed as having “non-functioning chromophobe adenomas.” All of the patients had visual field abnormalities and partial hypopituitarism. The elevated serum alpha concentrations showed
A, Klibanski, E C, Ridgway, N T, Zervas
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Reduction and reoxidation of equine gonadotropin alpha-subunits.

Endocrinology, 1992
Ovine (o) and equine (e) LH alpha-subunits were reduced and reoxidized using conditions known to be effective for bovine and human alpha-subunits. The major product of oLH alpha refolding was alpha-subunit monomer. In contrast, eLH alpha formed a 121,000 mol wt aggregate. Monomeric eLH alpha was recovered, but in greatly reduced yield.
Bousfield, George R., Ward, Darrell N.
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Evidence for oligomeric forms of transducins alpha subunit: Formation of intermolecular alpha-alpha disulfide linkages

Biochemical and Biophysical Research Communications, 1989
Transducin, the retinal G-protein, is a heterotrimeric protein composed of alpha, beta and gamma subunits. Intermolecular disulfide linkages between the alpha-subunits of transducin molecules are spontaneously formed when the purified G-protein is placed in a non-reducing buffer system.
M, Wessling-Resnick, G L, Johnson
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