Hemoglobins, crosslinked

Brucker EA. Genetically crosslinked hemoglobin a structural study. Acta Crys-tallogr D Biol Crystallogr 2000 56(Pt 7) 812. 

Nary, J. Ling, G. Lojeski, E. Muldoon, S. Traumatic brain injury in rats histopathologic effects of hemodilution with diaspirin crosslinked hemoglobin. Anesthe-siol 1997, 87 (3A), A 681. 

Davis, T. A., Asher, W. J., and Wallace, H. W., 1984, Artificial red blood cells with crosslinked hemoglobin membranes, ylpp/. Biochem. Biotechnol. 10 123-132. 

Ogle, K. F., and Azari, M. R. (2001). Vims removal by ultrafiltration A case study with diasprin crosslinked hemoglobin (DCLHb). In W. K. Wang (Ed.), Membrane Separations in Biotechnology. Marcel Dekker, New York, p. 299. 

Ulatowski, J.A., Nishikawa, T., Matheson-Urbaitis, B., Bucd, E., Traystman, R.J., and Koehler, R.C. Regional blood flow alterations after bovine fumaryl beta beta-crosslinked hemoglobin transfusion and nitric oxide synthase inhibition. Crit Care Med 24 558-565,1996. 

Kofinas et al. (1996) have prepared PEO hydrogels by a similar technique. In this work, they studied the diffusional behavior of two macromolecules, cytochrome C and hemoglobin, in these gels. They noted an interesting, yet previously unreported dependence between the crosslink density and protein diffusion coefficient and the initial molecular weight of the linear PEGs. 

The neurotoxic effects of -hexane have been associated with the pyrrolidation of protein (Graham et al. 1995) by 2,5-hexanedione. Therefore, the development of analytical methods to determine this potential biomarker of effect of -hexane in hair and the subsequent crosslinking of the blood proteins, spectrin and hemoglobin, would be useful. 

Chang TM. Modified hemoglobin-based blood substitutes crosslinked, recombinant and encapsulated hemoglobin. Vox Sang 74(suppl 2) 233, 1998. 

Fronticelli C, Sato T, Orth C, et al. Bovine hemoglobin as a potential source of hemoglobin-based oxygen carriers crosslinking with bis(2,3-dibromosalycyl)fu-marate. Biochim Biophys Acta 1986 874 76. 

Copper was recognized as nutritionally essential by 1924 and has since been found to function in many cellular proteins.470-474 Copper is so broadly distributed in foods that a deficiency has only rarely been observed in humans.4743 However, animals may sometimes receive inadequate amounts because absorption of Cu2+ is antagonized by Zn2+ and because copper may be tied up by molybdate as an inert complex. There are copper-deficient desert areas of Australia where neither plants nor animals survive. Copper-deficient animals have bone defects, hair color is lacking, and hemoglobin synthesis is impaired. Cytochrome oxidase activity is low. The protein elastin of arterial walls is poorly crosslinked and the arteries are weak. Genetic defects in copper metabolism can have similar effects. 

In view of the high affinity of arsenic for thiol functions, it can be expected that lewisite and CVAA will bind to cysteine residues of proteins. When human blood was incubated with 20 nM to 0.2 mM of [14C]lewisite, 25-50% of the dose became associated with globin (35). Electrospray tandem MS provided evidence for the presence of a CVAA-crosslink between the cysteine-93 and cysteine-112 residues in fi-globin. Whether this was the only type of adduct has not yet been completely elucidated. It must be remarked, however, that this result was in contrast with results obtained by others for the analogous phenyldichloroarsine, for which binding to human hemoglobin could not be observed. 

Chemical crosslinking of proteins in combination with mass spectroscopy is often used for the mapping of the three dimensional structures in proteins. An example is the crosslinking of hemoglobin. " The authors also studied the structures of crosslinked neurofibrillary tangles isolated from the brain of an Alzheimer s disease patient. 

Crosslinking of protein monolayers by mercuric ion (MacRitchie, 1970) and silicic acid (Minones et al., 1973) has been reported. These studies are relevant to poisoning by heavy-metal ions and to silicosis, effects that seem likely to result from attack on the cell membrane proteins. Crosslinking by mercuric ion was detected by a spectacular increase in surface viscosity and a decrease in compressibility when a number of proteins (BSA, insulin, ovalbumin, and hemoglobin) were spread on 0.001 M mercuric chloride solution. Poly-DL-alanine was unaffected whereas poly-L-lysine and poly-L-glutamic acid were affected in a similar manner to the proteins, indicating that mercuric ion interacts with the ionizable carboxyl and amino groups on the protein side—chains. Silicic acid similarly caused protein monolayers... 

Microperoxidase-11, MP-11, is a heme-undecapeptide that is prepared by the digestion of cytochrome c and it includes the active surrounding of cytochrome MP-11 was immobilized on electrode surface s and its electrochemistry was characterized. The MP-11-modified electrodes were reported to act as effective electron mediator interfaces for the reduction of cytochrome c, hemoglobin, myoglobin and nitrate reductase (cytochrome c-dependent). The MP-11-mediated activation of nitrate reductase, NR, was employed to assemble an integrated MP-11/NR electrode for the bioelectrocatalyzed reduction of nitrate (NO3 ) to nitrite (NO2). An affinity complex between a MP-11-functionalized electrode and NR (/Q = 3.7x10 M ) was crosslinked with glutaric dialdehyde to yield the electrically contacted electrode for the bioelectrocatalyzed reduction of nitrate to nitrite. In this system the reduced MP-11 mediates ET to NR and activates the enzyme towards the reduction of NO3. 

The cortex is an amorphous and electron-dense layer composed of at least two sublayers which are abundant in keratin-like proteins and a highly insoluble protein termed cuticulin. The medial layer is a fluid-filled compartment that also contains fine collagenous fibers. In some species, the fluid contains hemoglobin. The composite basal layer contains crosslinked collagen fibers in two to three distinct sublayers which spiral around the nematode at an angle 75° to the longitudinal axis. 

The glutaraldehyde difluses slowly through the oil to the surface of the microdroplets where the hemoglobin is crosslinked to form a new membrane. 

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