Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P11021 (BiP)
 2,049 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have developed a single purification procedure for the four major resident endoplasmic reticulum (ER) proteins: protein disulfide isomerase (PDI), BiP, endoplasmin, and calreticulin. Three of these proteins are thought to play a role in protein folding in vivo, whereas calreticulin is thought to be the major calcium binding protein in the ER. The proteins were purified from fresh bovine liver by taking advantage of individual characteristics of the proteins. Liver microsomes were prepared and then premeabilized to release the lumenal contents. After ammonium sulfate precipitation, the proteins were purified by chromatography; BiP was purified by affinity chromatography on ATP-agarose, and both endoplasmin and calreticulin were purified by affinity chromatography on Con A-Sepharose. PDI was purified by anionic ion exchange chromatography.
 ...
PMID:A single purification procedure for the major resident proteins of the ER lumen: endoplasmin, BiP, calreticulin and protein disulfide isomerase. 795 Mar 79

Intracellular distribution of selected reticuloplasmins, soluble proteins of the endoplasmic reticulum lumen, in rat mammary gland was investigated during pregnancy, lactation, and involution. During lactation the levels of the calcium binding protein calreticulin, and of protein disulfide isomerase, were elevated. Endoplasmic reticulum was as efficient as Golgi apparatus in sequestration and accumulation of Ca2+ from surrounding medium, as suggested from in vitro experiments with isolated cell fractions. Both protein disulfide isomerase and calreticulin were present in cytosol from homogenates of mammary gland prepared under mild conditions. Protein disulfide isomerase was abundant in intracellular lipid droplet precursors of milk lipid globules. Calreticulin and immunoglobulin binding protein (BiP, GRP 78) were associated with lipid droplets. Glucose-regulated protein (GRP 94) was not detected in association with intracellular lipid droplets. Milk lipid globule membrane lacked more than barely detectable quantities of protein disulfide isomerase, calreticulin, and immunoglobulin binding protein, suggesting that these proteins are lost from intracellular lipid droplets before or during their secretion as milk lipid globules. Immunocytochemical localization confirmed the presence of protein disulfide isomerase or calreticulin on intracellular lipid droplets and in non-endoplasmic reticulum regions of cells.
 ...
PMID:Endoplasmic reticulum lumenal proteins of rat mammary gland. Potential involvement in lipid droplet assembly during lactation. 803 38