Results 281 to 290 of about 66,240 (319)

Engineering the hydrophobic pocket of carbonic anhydrase II

Biochemistry, 1991
Wild-type and mutant human carbonic anhydrases II, where mutations have been made in the hydrophobic pocket of the active site, have been studied by X-ray crystallographic methods. Specifically, mutations at Val-143 (the base of the pocket) lead to significant changes in catalytic activity and protein structure.
R S, Alexander, S K, Nair, D W, Christianson   +2 more
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Amino acid sequence of rabbit carbonic anhydrase II

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
The amino acid sequence of the high activity form of erythrocyte carbonic anhydrase, carbonic anhydrase II, purified from rabbit erythrocytes has been determined. This sequence was determined primarily from the cyanogen bromide and tryptic peptides through use of automated Edman degradation procedures.
R E, Ferrell, S K, Stroup, R J, Tanis, R E, Tashian   +3 more
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Meningiomas: Role of Carbonic Anhydrase II

2012
Carbonic anhydrase (CA) II belongs to the family of metalloenzymes that catalyze the reversible hydration of carbon dioxide. It is widely distributed in normal organs and it is the main isoenzyme in the nervous system. In addition, CA II is expressed in several malignant tumors.
Katariina Korhonen, Silvia Pastorekova
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Ureidobenzenesulfonamides as efficient inhibitors of carbonic anhydrase II

Bioorganic Chemistry, 2019
Sulfonamides represent an important class of drugs because of their inhibitory effect on carbonic anhydrases (CAs). We therefore synthesized several ureidobenzenesulfonamides and evaluated their bCA II inhibition for their potential use as anti-glaucoma gents.
Immo, Serbian, Philipp, Schwarzenberger, Anne, Loesche, Sophie, Hoenke, Ahmed, Al-Harrasi, René, Csuk   +5 more
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Carbonic Anhydrase II Deficiency Syndrome

1991
Since osteopetrosis (marble bone disease) was first described by Albers-Schonberg in 1904, over 300 cases have been reported.5 An autosomal dominant form, the adult, benign form, has a relatively benign course and is compatible with a normal life span.
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Rapid Method for Differentiation of Carbonic Anhydrase I from Carbonic Anhydrase II Activity

Analytical Letters, 1999
ABSTRACT A simple method for differentiation of carbonic anhydrase (CA) I, from CA II, is described based on using the nicotinates as specific CA I inhibitors. Nicotinates inhibit the activity of CA I activity; at a concentration of 5x10−1M 100% inhibition is complete. But no effect on CA II activity is observed.
I. Puscas, Marcela Coltau, Gabriela Domuta   +2 more
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Carbonic anhydrase II does not exhibit Nitrite reductase or Nitrous Anhydrase Activity

Free Radical Biology and Medicine, 2018
Carbonic anhydrase II (CA II) is a zinc metalloenzyme that catalyzes the reversible interconversion of water and CO2 to bicarbonate and a proton. CA II is abundant in most cells, and plays a role in numerous processes including gas exchange, epithelial ion transport, respiration, extra- and intracellular pH control, and vascular regulation.
Jacob T, Andring, Carrie L, Lomelino, Chingkuang, Tu, David N, Silverman, Robert, McKenna, Erik R, Swenson   +5 more
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Carbonic anhydrases in meningiomas: association of endothelial carbonic anhydrase II with aggressive tumor features.

Journal of neurosurgery, 2009
Carbonic anhydrase (CA) II and IX are enzymes involved in pH homeostasis and have been shown to be upregulated in several types of cancer. In this study, the authors evaluate the expression of CA II and IX in meningiomas and assess their relationship to patient age, tumor type and grade, tumor sex hormone receptor status, tumor cell proliferation, and ...
Katariina, Korhonen, Anna-Kaisa, Parkkila, Pauli, Helen, Ritva, Välimäki, Silvia, Pastorekova, Jaromir, Pastorek, Seppo, Parkkila, Hannu, Haapasalo   +7 more
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Carbonic anhydrase II expression in rat type II pneumocytes.

American Journal of Respiratory Cell and Molecular Biology, 1994
Pulmonary carbonic anhydrase (CA) activity plays important roles in carbon dioxide exchange, fluid secretion, and pH regulation. This study reports the use of molecular and immunologic techniques to characterize expression of the high-activity cytosolic isoenzyme CA II in rat lung tissue.
R E, Fleming, M A, Moxley, A, Waheed, E C, Crouch, W S, Sly, W J, Longmore   +5 more
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Folding and stability of human carbonic anhydrase II

2000
Knowledge of various dynamic aspects of the structure of carbonic anhydrase is important for comprehension of the structural integrity and function of the enzyme. Therefore, characterization of the folding pathway will contribute to a deeper understanding of the structure-function relationship and will provide clues to help solve the protein folding ...
U, Carlsson, B H, Jonsson
openaire   +2 more sources