Video Experimental Relacionado
Updated: Jul 9, 2026

12:48
Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
Published on: February 19, 2013
Estructura primaria de la subunidad alfa de Torpedo californica (Na+ + K+) ATPasa deducida de la secuencia de ADNc
Nature
|August 22, 1985
Resumen
Los investigadores clonaron y secuenciaron la subunidad alfa de la ATPasa dependiente de sodio y potasio [Na+ + K+]. Esto proporciona la secuencia completa de aminoácidos para esta proteína clave de transporte activo.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- Biología celular Biología celular.
Sus antecedentes:
- La ATPasa dependiente de sodio y potasio [Na+ + K+] es vital para el transporte activo en las células animales.
- Esta enzima comprende subunidades alfa y beta; se cree que la subunidad alfa (Mr 84,000-120,000) es catalítica.
Objetivo del estudio:
- Clonar y secuenciar el ADN complementario al ARN mensajero que codifica la subunidad alfa de (Na+ + K+) ATPasa de Torpedo californica electroplax.
- Para deducir la secuencia completa de aminoácidos del polipéptido alfa-subunidad.
Principales métodos:
- La clonación del ADN complementario (ADNc). clonación del ADN complementario (ADNc).
- Secuenciación del ARN mensajero (ARNm). secuenciación del ARN mensajero (ARNm).
- Determinación de la secuencia de aminoácidos.
Principales resultados:
- Se clonó y secuenció con éxito el ADNc para la subunidad alfa de (Na+ + K+) ATPasa.
- Dedujo la secuencia completa de aminoácidos de la subunidad alfa.
Conclusiones:
- Se ha determinado la secuencia completa de aminoácidos de la subunidad alfa de (Na+ + K+) ATPasa.
- Se discuten las características estructurales relacionadas con la función de transporte activo de la enzima.
Videos de Conceptos Relacionados
ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
ATP Synthase: Structure
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
The ADP/ATP Carrier Protein
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
ATP Driven Pumps II: P-type Pumps
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

