The effect of tris (hydroxymethyl) aminomethane on membrane bound 5′-nucleotidase from swine aortic smooth muscle

Goldman, S J; Slakey, Linda L.

doi:10.1016/0005-2744(81)90261-8

Cited by 7 publications

(2 citation statements)

References 20 publications

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“…This activation is specific for Tris, and Tris analogues, such as Bistris or tricine, induce no such effect. Similar specific activations have also been observed in other proteins [24–30]. As shown in Fig.…”

Section: Resultssupporting

confidence: 87%

Crystal structure of salt‐tolerant glutaminase from Micrococcus luteus K‐3 in the presence and absence of its product l‐glutamate and its activator Tris

et al. 2010

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Glutaminase from Micrococcus luteus K‐3 [Micrococcus glutaminase (Mglu); 456 amino acid residues (aa); 48 kDa] is a salt‐tolerant enzyme. Our previous study determined the structure of its major 42‐kDa fragment. Here, using new crystallization conditions, we determined the structures of the intact enzyme in the presence and absence of its product l‐glutamate and its activator Tris, which activates the enzyme by sixfold. With the exception of a ‘lid’ part (26‐29 aa) and a few other short stretches, the structures were all very similar over the entire polypeptide chain. However, the presence of the ligands significantly reduced the length of the disordered regions: 41 aa in the unliganded structure (N), 21 aa for l‐glutamate (G), 8 aa for Tris (T) and 6 aa for both l‐glutamate and Tris (TG). l‐Glutamate was identified in both the G and TG structures, whereas Tris was only identified in the TG structure. Comparison of the glutamate‐binding site between Mglu and salt‐labile glutaminase (YbgJ) from Bacillus subtilis showed significantly smaller structural changes of the protein part in Mglu. A comparison of the substrate‐binding pocket of Mglu, which is highly specific for l‐glutamine, with that of Erwinia carotovora asparaginase, which has substrates other than l‐glutamine, shows that Mglu has a larger substrate‐binding pocket that prevents the binding of l‐asparagine with proper interactions. Structured digital abstract http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-7305730: Mglu (uniprotkb:http://www.uniprot.org/uniprot/Q4U1A6?format=text&ascii) and Mglu (uniprotkb:http://www.uniprot.org/uniprot/Q4U1A6?format=text&ascii) bind (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407) by x‐ray crystallography (http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0114)

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Section: Resultssupporting

confidence: 87%

Crystal structure of salt‐tolerant glutaminase from Micrococcus luteus K‐3 in the presence and absence of its product l‐glutamate and its activator Tris

et al. 2010

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“…5'-Nucleotidase and NADH-cytochrome c reductase (rotenone-insensitive) activities were measured as described by Wuytack et al (1978), except that for the measurement of 5'-nucleotidase the Tris buffer was replaced by glycine buffer, as suggested by Goldman & Slakey (1981).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Isolation of a plasma-membrane fraction from gastric smooth muscle. Comparison of the calcium uptake with that in endoplasmic reticulum

Raeymaekers¹,

Wuytack²,

Eggermont³

et al. 1983

Biochemical Journal

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1. A plasma-membrane fraction was isolated from the smooth muscle of the pig stomach by using differential and sucrose-density-gradient centrifugations. When the centrifugation was carried out after preloading the crude microsomal fraction with Ca2+ in the presence of oxalate, the contamination of the plasma-membrane fraction by endoplasmic reticulum was decreased and a fraction enriched in endoplasmic reticulum vesicles filled with calcium oxalate crystals was obtained. 2. The plasmalemmal and endoplasmic-reticulum membranes could be distinguished by differences in the activity of marker enzymes and in the cholesterol content and by their different permeability to oxalate and phosphate. Oxalate and phosphate stimulated the Ca2+ uptake in the endoplasmic reticulum much more than in the plasmalemmal vesicles. In the plasma-membrane vesicles 40 mM-phosphate was more effective for stimulating the Ca2+ uptake than was 5 mM-oxalate, but the reverse was seen in the endoplasmic reticulum. 3. The high cholesterol/phospholipid ratio of the crude microsomal fraction are of the majority of the vesicles present in the crude microsomal fraction are of plasmalemmal origin. 4. The Ca2+ pump of the plasmalemmal and endoplasmic-reticulum vesicles could be differentiated by their different sensitivities to calmodulin. However, the two Ca2+-transport ATPases did not differ by their sensitivity to vanadate nor by the energization of the Ca2+ transport by different nucleoside triphosphates.

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Transfer of tris buffer and effects on K+ loss in human red blood cells and reconstituted ghosts

Bodemann

Karsch

1984

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The effect of tris (hydroxymethyl) aminomethane on membrane bound 5′-nucleotidase from swine aortic smooth muscle

Cited by 7 publications

References 20 publications

Crystal structure of salt‐tolerant glutaminase from Micrococcus luteus K‐3 in the presence and absence of its product l‐glutamate and its activator Tris

Crystal structure of salt‐tolerant glutaminase from Micrococcus luteus K‐3 in the presence and absence of its product l‐glutamate and its activator Tris

Isolation of a plasma-membrane fraction from gastric smooth muscle. Comparison of the calcium uptake with that in endoplasmic reticulum

Transfer of tris buffer and effects on K+ loss in human red blood cells and reconstituted ghosts

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