Protein storage

Arachin, the counterpart of glycinin in peanuts, consists of subunits of 60,000—70,000 mol wt which on reduction with 2-mercaptoethanol yield polypeptides of 41,000—48,000 and 21,000 mol wt (17) analogous to the behavior of glycinin. In addition to the storage proteins, oilseeds contain a variety of minor proteins, including trypsin inhibitors, hemagglutinins, and enzymes. Examples of the last are urease and Hpoxygenase in soybeans. 

A. M. Altschul and H. L. Wilcke, eds., NeiP Protein Foods, Vol. 5, Seed Storage Proteins, Academic Press, Inc., New York, 1985, 471 pp. 

Cyprid major protein is a larval storage protein necessary for successful metamorphosis. " Production of cyprid major protein was increased in the barnacle Balanus amphitrite following exposure to both nonylphenol and estradiol, suggesting that it may be a potential biomarker of estrogen exposure in invertebrates such as barnacles. " "... 

Storage proteins Ovalbumin Casein Zein Phaseolin Eerritin... 

Calsequestrin is the major calcium storage protein of the sarcoplasmic reticulum in skeletal and cardiac muscles. It is highly acidic and has a large capacity for Ca2+. Calsequestrin functions to localize calcium near the junctional face of the terminal cistemae from which calcium can be released into the cytosol via the ryanodine receptor. 

Molybdenum hexafluoride. 3,1412 Molybdenum-iron-sulfur complexes, 4,241 Molybdenum oxide amino acid formation prebiotic systems, 6, 872 Molybdenum storage protein microorganisms, 6, 681 Molybdenum telluride, 3, 1431 Molybdenum tetraalkoxides physical properties, 2, 347 Molybdenum tribromide, 3,1330 Molybdenum trichloride, 3,1330 Molybdenum trifluoride, 3, 1330 Molybdenum trihalides, 3, 1330 bond lengths, 3, 1330 magnetic moments, 3,1330 preparation, 3,1330 properties, 3, 1330 structure, 3,1330 Molybdenum triiodide, 3,1330 Molybdenum trioxide complexes, 3, 1379 Molybdenum triselenide, 3, 143)... 

Ferritin is a globular iron-storage protein that stores iron as FeJ+. To leave the ferritin, Fe3+ must first be reduced to Fe2+. Ferritin has two types of channels through which the Fe"+ could leave a three-fold channel and a four-fold channel. The three-fold channel is lined with the amino acids aspartate (Asp) and glutamate (Glu) and the four-fold channel is lined with the amino acid leucine (Leu). Through which channel is the Fe + more likely to leave the ferritin protein Explain your answer. 

Schematic representation of ferritin, the iron storage protein, (a) The protein contains 24 neariy identical polypeptides, (b) A ribbon stmcture of one of the polypeptide chains.

C20-0105. The iron storage protein ferritin usuaiiy is neither empty of iron nor fiiied to capacity. Why is this situation advantageous for an organism ... 

CARBONARO M, GRANT G, CAPPELLONi M, puszTAi A (2000) Perspectives into factors limiting in vivo digestion of legume proteins antinutritional compormds or storage proteins JAgric Food Chem. 48 742-9. 

Rosahl S, Schmidt R, Schell J, Willmitzer L (1986) Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein in potato tubers. Mol Gen Genet 203 214-220... 

Aisen, P. and Listowsky, I. (1980). Iron transport and storage proteins. Annu. Rev. Bitx hem. 49, 357-393. 

Figure 6.13 shows the Mossbauer spectra of ferritin [51], which is an iron-storage protein consisting of an iron-rich core with a diameter around 8 nm with a structure similar to that of ferrihydrite and which is surrounded by a shell of organic material. At 4.2 K essentially all particles contribute to a magnetically split component, but at higher temperatures the spectra show the typical superposition of a doublet and a sextet with a temperature dependent area ratio. At 70 K the sextet has disappeared since all particles have fast superparamagnetic relaxation at this temperature. 

Finally, animal, plant and microbial tissues have been shown to contain the iron storage protein ferritin. The animal protein has been extensively studied, but the mechanism of iron binding has not been completely resolved (29). Animal tissues contain, in addition, a type of granule comprised of iron hydroxide, polysaccharide and protein. The latter, called hemosiderin, may represent a depository of excess iron (30). Interestingly, a protein with properties parallel to those of ferritin has been found in a mold. Here the function of the molecule can be examined with the powerful tools of biochemical genetics (31). 

Oxygen transport and storage proteins Heme proteins ... 

The core of the iron storage protein ferritin consists of a hydrated ferric oxide-phosphate complex. Various models have been proposed which feature Fe111 06 oct., Fe111 O4 tet. or Fe111 O4 tet. Fe111 06 oct. complexing the first listed is preferred by Gray (99) on the basis of the electronic absorption spectrum. The protein very closely related to ferritin which occurs in the mold Phycomyces blakesleeanus contains... 

In the absence of a demonstrable yeast iron-storage protein (ferritin), we have to recognize that, despite our substantial advances in understanding iron uptake in yeast, we know practically nothing about intracellular iron metabolism - except that is for iron transport into, and out of, mitochondria. 

Cu is bound by a /3-sheet protein (enzyme) in 3 or 4 coordination using histidines or/and cysteines. Cu+ is bound by thiolates in storage proteins. 

The iron storage protein ferritin is a small 20 kDa a-helical protein that spontaneously assembles into a hollow ball-like homo-24-mer. The outer diameter of the sphere is circa 12 nm and the inner diameter, or core diameter, is circa 8 nm. A smaller version, known as miniferritin or Dps protein (Dps = DNA protecting... 

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