Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Proteins iron and

Mossbauer spectra of the reduced proteins in the above study are not consistent with subsequent data for these proteins (153,164,165). It is now believed (personal communications, W. H. Orme-Johnson and Graham Palmer) that 1, the samples in these experiments were impure, and 2. the buffers used in these experiments were not strong enough to maintain a buffer pH level during the dithionite reductions. Therefore, the Mossbauer spectra of reduced spinach ferredoxin in the above experiment resulted from a mixture of oxodized protein iron and iron from denatured protein material. [Pg.25]

An excellent source of complete protein, iron, and other minerals... [Pg.629]

Clinical chemistry and toxicology are also known as clinical biochemistry or clinical pathology, and they utilize a variety of analytical procedures to analyze body fluids to aid in medical prevention, diagnosis and treatment. Analytes commonly targeted include electrolytes, creatinine, albumin and other proteins, iron and prescription (therapeutic) and illicit drugs. [Pg.1]

Compared to the rooB, the cooked greens com lain about the same amounts of water and cal-oiies, but twice as much protein, iron, and vitamin C, and many times as much vitamin A lof which they are an axcaleni sourcel. [Pg.1053]

Spices and herbs can play an important indirect role in good nutrition. They are not high in nutrient values, but they help to increase the appeal and satisfaction of foods that are highly nutritious. Spices do contain fat, protein and carbohydrates, electrolytic minerals, iron and B vitamins, and others, but even the highest calorie spice, poppy seeds, contains only two to three calories per serving in normal use (12). [Pg.27]

The dopamine is then concentrated in storage vesicles via an ATP-dependent process. Here the rate-limiting step appears not to be precursor uptake, under normal conditions, but tyrosine hydroxylase activity. This is regulated by protein phosphorylation and by de novo enzyme synthesis. The enzyme requites oxygen, ferrous iron, and tetrahydrobiopterin (BH. The enzymatic conversion of the precursor to the active agent and its subsequent storage in a vesicle are energy-dependent processes. [Pg.517]

Proteins and Meals. Nutritional properties of the oilseed protein meals and their derived products are deterrnined by the amino acid compositions, content of biologically active proteins, and various nonprotein constituents found in the defatted meals. Phytic acid (3), present as salts in all four meals, is beheved to interfere with dietary absorption of minerals such as 2inc, calcium, and iron (67) (see Food toxicants, naturally occurring Mineral nutrients). ... [Pg.301]

The side chains of the 20 different amino acids listed in Panel 1.1 (pp. 6-7) have very different chemical properties and are utilized for a wide variety of biological functions. However, their chemical versatility is not unlimited, and for some functions metal atoms are more suitable and more efficient. Electron-transfer reactions are an important example. Fortunately the side chains of histidine, cysteine, aspartic acid, and glutamic acid are excellent metal ligands, and a fairly large number of proteins have recruited metal atoms as intrinsic parts of their structures among the frequently used metals are iron, zinc, magnesium, and calcium. Several metallo proteins are discussed in detail in later chapters and it suffices here to mention briefly a few examples of iron and zinc proteins. [Pg.11]

Three protein complexes have been isolated, including the flavoprotein (FP), iron-sulfur protein (IP), and hydrophobic protein (HP). FP contains three peptides (of mass 51, 24, and 10 kD) and bound FMN and has 2 Fe-S centers (a 2Fe-2S center and a 4Fe-4S center). IP contains six peptides and at least 3 Fe-S centers. HP contains at least seven peptides and one Fe-S center. [Pg.683]

As well as donating electrons to the MoFe protein, the Fe protein has at least two and possibly three other functions (see Section IV,C) It is involved in the biosynthesis of the iron molybdenum cofactor, FeMoco it is required for insertion of the FeMoco into the MoFe protein polypeptides and it has been implicated in the regulation of the biosynthesis of the alternative nitrogenases. [Pg.164]

CODH/ACS is an extremely oxygen-sensitive protein that has been found in anaerobic microbes. It also is one of the three known nickel iron-sulfur proteins. Some authors would consider that there are only two, since the CODH and ACS activities are tightly linked in many organisms. However, there is strong evidence that the ACS and CODH activities are associated with different protein subunits and the reactions that the two enzymes catalyze are quite different. CODH catalyzes a redox reaction and ACS catalyzes the nonredox condensation of a methyl group, a carbonyl group, and an organic thiol (coenzyme A). [Pg.305]

A preliminaiy characterization of a new iron—sulfur protein isolated from Desulfovibrio vulgaris Hildenborough was reported in 1989 124). The protein contained approximately 6 iron and 6 inorganic sulfur atoms per molecule. The FPR spectrum of the dithionite reduced protein exhibited an S = signal similar to what was found for synthetic compounds with a [6Fe-6S] core (prismane core). No other FPR signals were reported at this time, and based on the observed similarity it was suggested that this peculiar iron-sulfur protein contained a [6Fe-6S] cluster. Because it had no known function, the pro-... [Pg.378]

A number of iron-containing, ascorbate-requiring hydroxylases share a common reaction mechanism in which hydroxylation of the substrate is linked to decarboxylation of a-ketoglutarate (Figure 28-11). Many of these enzymes are involved in the modification of precursor proteins. Proline and lysine hydroxylases are required for the postsynthetic modification of procollagen to collagen, and prohne hydroxylase is also required in formation of osteocalcin and the Clq component of complement. Aspartate P-hydroxylase is required for the postsynthetic modification of the precursor of protein C, the vitamin K-dependent protease which hydrolyzes activated factor V in the blood clotting cascade. TrimethyUysine and y-butyrobetaine hydroxylases are required for the synthesis of carnitine. [Pg.496]

There are receptors (TfRs) on the surfaces of many cells for transferrin, it binds to these receptors and is internalized by receptor-mediated endocytosis (compare the fate of LDL Chapter 25). The acid pH inside the lysosome causes the iron to dissociate from the protein. The dissociated iron leaves the endosome via DMTl to enter the cytoplasm. Unlike the protein component of LDL, apoTf is not degraded within the lysosome. Instead, it remains associated with its receptor, returns to the plasma membrane, dissociates from its receptor, reenters the plasma, picks up more iron, and again delivers the iron to needy ceils. [Pg.586]

Ferritin is another protein that is important in the metabolism of iron. Under normal conditions, it stores iron that can be called upon for use as conditions require. In conditions of excess iron (eg, hemochromatosis), body stores of iron are greatly increased and much more ferritin is present in the tissues, such as the liver and spleen. Ferritin contains approximately 23% iron, and apoferritin (the protein moiety free of iron) has a molecular mass of approximately 440 kDa. Ferritin is composed of 24 subunits of 18.5 kDa, which surround in a micellar form some 3000-4500 ferric atoms. Normally, there is a little ferritin in human plasma. However, in patients with excess iron, the amount of ferritin in plasma is markedly elevated. The amount of ferritin in plasma can be conveniently measured by a sensitive and specific radioimmunoassay and serves as an index of body iron stores. [Pg.586]

Lactoferrin j Iron-binding protein May inhibit growth of certain bacteria by binding iron and may be involved in regulation of proliferation of myeloid cells... [Pg.621]

New information has been added in appropriate chapters on hpid rafts and caveolae, aquaporins, connexins, disorders due to mutations in genes encoding proteins involved in intracellular membrane transport, absorption of iron, and conformational diseases and pharmacogenomics. [Pg.699]


See other pages where Proteins iron and is mentioned: [Pg.290]    [Pg.277]    [Pg.290]    [Pg.277]    [Pg.1148]    [Pg.383]    [Pg.274]    [Pg.462]    [Pg.121]    [Pg.129]    [Pg.454]    [Pg.1148]    [Pg.1198]    [Pg.29]    [Pg.324]    [Pg.264]    [Pg.3]    [Pg.84]    [Pg.106]    [Pg.160]    [Pg.164]    [Pg.176]    [Pg.177]    [Pg.195]    [Pg.199]    [Pg.210]    [Pg.219]    [Pg.370]    [Pg.380]    [Pg.450]    [Pg.457]    [Pg.474]    [Pg.274]    [Pg.1429]    [Pg.1481]   
See also in sourсe #XX -- [ Pg.157 , Pg.250 , Pg.267 , Pg.268 , Pg.269 ]




SEARCH



Iron protein proteins

© 2024 chempedia.info