Preparation and Pore Structure of Energy-Storage Phosphorus Building Gypsum.

In this study, the pore structure of a hardened phosphorous building gypsum body was optimised by blending an air-entraining agent with the appropriate water-paste ratio. The response surface test was designed according to the test results of the hardened phosphorous building gypsum body treated with an air-entraining agent and an appropriate water-paste ratio. Moreover, the optimal process parameters were selected to prepare a porous phosphorous building gypsum skeleton, which was used as a paraffin carrier to prepare energy-storage phosphorous building gypsum.

Amino Acids 785, 787 of the Na/H Exchanger Cytoplasmic Tail Modulate Protein Activity and Tail Conformation.

The mammalian Na/H exchanger isoform 1 (NHE1) is a plasma membrane protein ubiquitously present in humans. It regulates intracellular pH by removing an intracellular proton in exchange for an extracellular sodium. It consists of a 500 amino acid membrane domain plus a 315 amino acid, regulatory cytosolic tail.

Acidic residues of extracellular loop 3 of the Na/H exchanger type 1 are important in cation transport.

Mammalian Na/H exchanger type I isoform (NHE1) is a ubiquitously expressed membrane protein that regulates intracellular pH (pHi) by removing one intracellular proton in exchange for one extracellular sodium ion. Abnormal activity of the protein occurs in cardiovascular disease and breast cancer. The purpose of this study is to examine the role of negatively charged amino acids of extracellular loop 3 (EL3) in the activity of the NHE protein.

Diverse residues of intracellular loop 5 of the Na/H exchanger modulate proton sensing, expression, activity and targeting.

The mammalian Na/H exchanger isoform 1 (NHE1) is an integral membrane protein that regulates intracellular pH (pH) by removing a single intracellular proton in exchange for one extracellular sodium ion. It is involved in cardiac hypertrophy and ischemia reperfusion damage to the heart and elevation of its activity is a trigger for breast cancer metastasis. NHE1 has an extensive 500 amino acid N-terminal membrane domain that mediates transport and consists of 12 transmembrane segments connected by intracellular and extracellular loops.