Identification of subunit contact sites on the .alpha.-subunit of lutropin

Biochemistry ◽  
1991 ◽  
Vol 30 (7) ◽  
pp. 1858-1864 ◽  
Author(s):  
Stanley R. Krystek ◽  
James A. Dias ◽  
Thomas T. Andersen
Keyword(s):  
Alpha Subunit ◽  
Contact Sites ◽  
Subunit Contact

scholarly journals Mapping the  70 subunit contact sites on Escherichia coli RNA polymerase with a  70-conjugated chemical protease

1998 ◽  
Vol 95 (11) ◽  
pp. 6021-6026 ◽  
Author(s):  
J. T. Owens ◽  
R. Miyake ◽  
K. Murakami ◽  
A. J. Chmura ◽  
N. Fujita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Contact Sites ◽  
Subunit Contact

scholarly journals Molecular Assembly of the Influenza Virus RNA Polymerase: Determination of the Subunit-Subunit Contact Sites

1996 ◽  
Vol 77 (9) ◽  
pp. 2149-2157 ◽  
Author(s):  
T. Toyoda ◽  
D. M. Adyshev ◽  
M. Kobayashi ◽  
A. Iwata ◽  
A. Ishihama
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Molecular Assembly ◽  
Contact Sites ◽  
Virus Rna ◽  
Subunit Contact

Structure of contact sites between the outer and inner mitochondrial membranes investigated by HVEM tomography

1996 ◽  
Vol 54 ◽  
pp. 966-967
Author(s):  
C.A. Mannella ◽  
K.F. Buttle ◽  
K.A. O‘Farrell ◽  
A. Leith ◽  
M. Marko
Keyword(s):  
Liver Mitochondrion ◽  
Adenine Nucleotide ◽  
Protein Complexes ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Contact Sites ◽  
Transmission Electron ◽  
Precursor Proteins ◽  
Membrane Contacts ◽  
And Function

Early transmission electron microscopy of plastic-embedded, thin-sectioned mitochondria indicated that there are numerous junctions between the outer and inner membranes of this organelle. More recent studies have suggested that the mitochondrial membrane contacts may be the site of protein complexes engaged in specialized functions, e.g., import of mitochondrial precursor proteins, adenine nucleotide channeling, and even intermembrane signalling. It has been suggested that the intermembrane contacts may be sites of membrane fusion involving non-bilayer lipid domains in the two membranes. However, despite growing interest in the nature and function of intramitochondrial contact sites, little is known about their structure.We are using electron microscopic tomography with the Albany HVEM to determine the internal organization of mitochondria. We have reconstructed a 0.6-μm section through an isolated, plasticembedded rat-liver mitochondrion by combining 123 projections collected by tilting (+/- 70°) around two perpendicular tilt axes. The resulting 3-D image has confirmed the basic inner-membrane organization inferred from lower-resolution reconstructions obtained from single-axis tomography.

Transient Prealbumin- Associated Hyperthyroxinemia in TSH-Producing Pituitary Adenoma

1990 ◽  
Vol 29 (01) ◽  
pp. 40-43 ◽  
Author(s):  
W. Langsteger ◽  
P. Költringer ◽  
P. Wakonig ◽  
B. Eber ◽  
M. Mokry ◽  
...  
Keyword(s):  
Computed Tomography ◽  
Case Report ◽  
Pituitary Adenoma ◽  
Thyroid Hormones ◽  
Protein Binding ◽  
Alpha Subunit ◽  
Normal Range ◽  
Thyroxine Binding Globulin ◽  
Free Thyroid Hormones ◽  
Transmission Computed Tomography

This case report describes a 38-year-old male who was hospitalized for further clarification of clinically mild hyperthyroidism. His increased total hormone levels, the elevated free thyroid hormones and the elevated basal TSH with blunted response to TRH strongly suggested a pituitary adenoma with inappropriate TSH incretion. Transmission computed tomography showed an intrasellar expansion, 16 mm in diameter. The neoplastic TSH production was confirmed by an elevated alpha-subunit and a raised molar alpha-sub/ATSH ratio. However, T4 distribution on prealbumin (PA, TTR), albumin (A) and thyroxine binding globulin (TBG) showed a clearly increased binding to PA (39%), indicating additional prealbumin-associated hyperthyroxinemia. The absolute values of PA, A and TBG were within the normal range. After removal of the TSH-producing adenoma, basal TSH, the free thyroid hormones and T4 binding to prealbumin returned to normal. Therefore, the prealbumin-associated hyperthyroxinemia had to be interpreted as a transitory phenomenon related to secondary hyperthyroidism (T4 shift from thyroxine binding globulin to prealbumin) rather than a genetically conditioned anomaly of protein binding.

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