scholarly journals Assembly of the (Na+ + K+)-adenosine triphosphatase. Post-translational membrane integration of the alpha subunit.

1984 ◽  
Vol 259 (4) ◽  
pp. 2629-2635 ◽  
Author(s):  
A Hiatt ◽  
A A McDonough ◽  
I S Edelman
Keyword(s):  
Adenosine Triphosphatase ◽  
Alpha Subunit

scholarly journals Loss of protection by nucleotides against proteolysis and thiol modification in the isolated α-subunit from F1 ATPase of Escherichia coli mutant uncA401

1984 ◽  
Vol 224 (1) ◽  
pp. 145-151 ◽  
Author(s):  
H Stan-Lotter ◽  
P D Bragg
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Alpha Subunit ◽  
Thiol Groups ◽  
Α Subunit ◽  
Partial Protection ◽  
E Coli ◽  
F1 Atpase ◽  
High Affinity ◽  
High Affinity Site

Binding of nucleotides to the high-affinity site of the isolated alpha subunit of normal Escherichia coli F1 adenosine triphosphatase (ATPase) results in partial protection against digestion by trypsin [Senda, Kanazawa, Tsuchiya & Futai (1983) Arch. Biochem. Biophys. 220, 398-440]. In contrast, the isolated alpha subunit from the defective ATPase of the E. coli uncA401 mutant (strain AN120) is cleaved by trypsin to peptides of less than 8000 Da in the presence of ADP or ATP (2.5 microM-110 mM). The nucleotide-dependent accessibility of thiol groups of the isolated alpha subunit was also studied. Two out of four thiol groups of the alpha subunit from normal ATPase are labelled by fluorescent maleimides or iodoacetates, but in the presence of ADP or ATP (0.14-1.2 mM), reaction of thiol groups with these labels is almost absent. Mutant alpha subunit, however, is labelled by these reagents at all four thiol groups in the presence or absence of ADP or ATP (1 mM). These results suggest that the mutation in the ATPase of strain AN120 leads either to the loss of the high-affinity nucleotide-binding site or affects transmission of allosteric changes that occur on binding of nucleotide to the isolated alpha subunit.

Immunochemistry of membrane F1-Adenosine triphosphatase fromMicrococcus lysodeikticus. Role of the alpha subunit

1981 ◽  
Vol 5 (6) ◽  
pp. 363-366 ◽  
Author(s):  
Vicente Larraga ◽  
Faustino Mollinedo ◽  
Emilio Muñoz
Keyword(s):  
Adenosine Triphosphatase ◽  
Alpha Subunit

scholarly journals The uncA gene codes for the α-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains

1979 ◽  
Vol 180 (1) ◽  
pp. 103-109 ◽  
Author(s):  
A E Senior ◽  
J A Downie ◽  
G B Cox ◽  
F Gibson ◽  
L Langman ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ionic Strength ◽  
Adenosine Triphosphatase ◽  
Alpha Subunit ◽  
Subunit Structure ◽  
Net Charge ◽  
Α Subunit ◽  
F1 Atpase ◽  
Mutant Strains ◽  
Low Ionic Strength

Four mutant strains of Escherichia coli which lack membrane-bound adenosine triphosphatase activity were shown by genetic-complementation tests to carry mutations in the uncA gene. A soluble inactive F1-ATPase aggregate was released from the membranes of three of the uncA mutant strains by low-ionic-strength washing, and purified by procedures developed for the purification of F1-ATPase from normal strains. Analysis of the subunit structure by two-dimensional gel electrophoresis indicated that the F1-ATPase in strains carrying the uncA401 or uncA453 alleles had a subunit structure indistinguishable from normal F1-ATPase. In contrast, the F1-ATPase from the strain carrying the uncA447 allele contained an alpha-subunit of normal molecular weight, but abnormal net charge. Membranes from strains carrying the uncA450 allele did not have F1-ATPase aggregates that could be solubilized by low-ionic-strength washing. However, a partial dipolid strain carrying both the uncA+ and uncA450 alleles formed an active F1-ATPase aggregate which could be solubilized by low-ionic-strength washing of the membranes and which contained two types of alpha-subunit, one of which was normal and the other had abnormal net charge. It is concluded that the uncA gene codes for the alpha-subunit of the adenosine triphosphatase.

Evidence for an allelic association between bipolar disorder and a Na+, K+ adenosine triphosphatase alpha subunit gene (ATP1A3)

1998 ◽  
Vol 44 (1) ◽  
pp. 47-51 ◽  
Author(s):  
Lesley Mynett-Johnson ◽  
Valerie Murphy ◽  
James McCormack ◽  
Denis C Shields ◽  
Eileen Claffey ◽  
...  
Keyword(s):  
Bipolar Disorder ◽  
Adenosine Triphosphatase ◽  
Alpha Subunit ◽  
Allelic Association ◽  
Subunit Gene

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

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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