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'Hemoglobin' in keywords

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1	Author	M. I. Oshtrakh, O. B. Milder, V. A. Semionkin, A. L. Berkovsky, M. A. Azhigirova, E. P. Vyazova	Requires cookie*
	Title	Variation of Quadrupole Splitting in Modified Oxyhemoglobin: A Mössbauer Effect Study
	Abstract	Human adult hemoglobin modified by both pyridoxal-5'-phosphate and glutaraldehyde in the oxy-form was studied by Mössbauer spectroscopy. Mössbauer spectra were measured at 87 and 295 K (hemoglobin in lyophilized form) and at 87 K (hemoglobin in frozen solution). The values of the quadrupole splitting for modified oxyhemoglobin were found to be lower then those of oxyhemoglobin without modifications in lyophilized form and frozen solution, respectively. The Mössbauer spectra of modified oxyhemoglobin were also analyzed in terms of the heme iron inequivalence in a-and /3-subunits of the tetramer. Differences of the tendencies of temperature dependencies of quadrupole splitting for modified and non-modified oxyhemoglobin in lyophilized form were shown.
	Reference	Z. Naturforsch. 55a, 193—198 (2000); received September 11 1999
	Published	2000
	Keywords	Hemoglobin, Mössbauer Spectroscopy, Quadrupole Spitting
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	TEI-XML for	default:Reihe_A/55/ZNA-2000-55a-0193.pdf
	Identifier	ZNA-2000-55a-0193
	Volume	55

2	Author	Meeno Jahan, Aftab Ahmed, Gerhard Braunitzer, ZafarH. Zaidi, H.E J, Reinhard Göltenboth	Requires cookie*
	Title	Carnivora: The Primary Structures of Adult Lion (Panthern leo) Hemoglobins
	Abstract	Complete amino acid sequences of lion (Panthera leo) hemoglobins are reported. Polyacryl amide gel disc electrophoresis at pH 8.3 and also in the presence of 8 M urea and Triton-X100, RP-HPLC, liquid and gas phase amino acid sequenator. and FAB Mass spectrometer are used. Sequences are aligned with human hemoglobin (Hb A) and compared with other hemoglobins of felidae.
	Reference	Z. Naturforsch. 42b, 1465 (1987); received July 23 1987
	Published	1987
	Keywords	Lion, Hemoglobin, HPLC, Primary Structure
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	TEI-XML for	default:Reihe_B/42/ZNB-1987-42b-1465.pdf
	Identifier	ZNB-1987-42b-1465
	Volume	42

3	Author	Nicholas Zagris, CharlesG. Melton	Requires cookie*
	Title	Hemoglobins in Single Chick Erythrocytes as Determined by a Differential Elution Procedure
	Abstract	The switch from embryonic to adult hemoglobin (Hb) has been studied in vivo by a correlated cytological and electrophoretic analysis of circulating red blood cells from early, purely embryonic-Hb stages to purely adult-Hb stages including the adult chicken. It has been discovered, by using an acid buffer treatment that selectively elutes adult but not embryonic Hb from intact red blood cells, that embryonic and adult Hbs occur together in single cells, and that the switch occurs simultaneously in all cells. These results together with knowledge of the chick erythroid cell dynamics and ontogenetic titers indicate that the initiation of adult Hb synthesis occurs in the circulation in cells previously committed only to embryonic Hb synthesis.
	Reference	Z. Naturforsch. 33c, 330 (1978); received January 17/March 10 1978
	Published	1978
	Keywords	Chick, Erythrocyte, Hemoglobins, Selective Elution
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	TEI-XML for	default:Reihe_C/33/ZNC-1978-33c-0330.pdf
	Identifier	ZNC-1978-33c-0330
	Volume	33

4	Author	Aftab Ahmed, Meeno Jahan, Gerhard Braunitzer, Reinhard Göltenboth	Requires cookie*
	Title	Carnivora: The Primary Structure of the Major and Minor Hemoglobin Components of Adult North Persian Leopard (Panthera pardus sexicolor)
	Abstract	The complete primary structure of the two hemoglobin components of the adult North Persian Leopard are presented. The major component Hb-I accounts for 80—90% and the minor compo-nent Hb-II accounts for 20—10% of the total hemoglobin. Reversed phase HPLC was used for the separation of the polypeptide chains. The amino acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-and gas-phase sequenators. The sequences are aligned with those of human Hb-A. Our result shows that the hemoglobins of North Persian Leopard and Jaguar are identical in amino acid sequence.
	Reference	Z. Naturforsch. 43b, 1341—1346 (1988); received May 24 1988
	Published	1988
	Keywords	Leopard, Hemoglobin, Primary Structure, Identical Chains
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	TEI-XML for	default:Reihe_B/43/ZNB-1988-43b-1341.pdf
	Identifier	ZNB-1988-43b-1341
	Volume	43

5	Author	H. L. Casal, U. Köhler, H. H. Mantsch, F.M G Oñ, J.L R Arrondo	Requires cookie*
	Title	Conformational Changes in Proteins Induced by Low Temperatures: an Infrared Study
	Abstract	Infrared spectra of hemoglobin (met-hemoglobin) and myoglobin were recorded in the temperature range —110 °C to 30 °C. On cooling hydroalcoholic solutions of hemoglobin, the spectra indicate a conformational change (revealed by the appearance of a band at 1665 cm ') com patible with the appearance of distortions in its a-helical structure. In the case of myoglobin smaller effects are ob served. These conformational changes are entirely revers ible and do not occur in frozen aqueous solutions.
	Reference	Z. Naturforsch. 42c, 1339—1342 (1987); received July 20/August 17 1987
	Published	1987
	Keywords	Hemoglobin, Myoglobin, Protein Conformation, FT-IR Cryobiology
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	TEI-XML for	default:Reihe_C/42/ZNC-1987-42c-1339_n.pdf
	Identifier	ZNC-1987-42c-1339_n
	Volume	42

6	Author	F. A. Bieber, H. Aschauer, S. M. Bektas, G. Braunitzer	Requires cookie*
	Title	Embryonale Hämoglobine der Säuger: Die Sequenzen der s-und ^-Ketten vom Hausschwein {Sus scrofa domestica) Embryonic Hemoglobins in Mammals: The Primary Structures o f e-and 5-Chains of the Pig (Sus scrofa dom estica)
	Abstract	The amino-acid sequences of all expressed hemoglobins of the pig embryo are given: Hemo globin Gower I (C2/e 2), Hemoblobin Gower II (oc2/ e 2), Hemoglobin Heide I (C2/>92) and Hemo globin Heide II (a2/<92). The e-and 5-chains were obtained with chromatography on CM-cellu-lose from isolated hemoglobin components. The primary structure was established by sequencing the tryptic peptides in the sequenator: they were isolated using HPLC. The C-chains from pig and human differ in 23, the e-chains in 20 positions. The embryonic globin-gene which express the 5-chains, is a new one in mammals, of e-type and up to now it could only be found in pigs: the amino-acid sequence differ in only 4 positions from the e-chains. Because no y-chains (fetal Hb) are expressed the sequences of all hemoglobins (5 hemoglobin chains forming 5 different hemo globins) of ontogeny in pig are now described.
	Reference	Z. Naturforsch. 38c, 613—616 (1983); eingegangen am 24. Februar 1983
	Published	1983
	Keywords	Hemoglobin, Pig Embryo, Sequences of (-, e-and9-Chains
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	TEI-XML for	default:Reihe_C/38/ZNC-1983-38c-0613.pdf
	Identifier	ZNC-1983-38c-0613
	Volume	38

7	Author	M. I. Oshtrakh	Requires cookie*
	Title	Mössbauer Effect in Biomedical Research: Variations of Quadrupole Splitting in Relation to the Qualitative Changes of Biomolecules
	Abstract	This review deals with studies of the variations of quadrupole splitting, electronic structure and stereochemistry of iron associated with qualitative changes of biomolecules. The possibility to determine various iron containing species resulting from the destruction of biomolecules using Mössbauer parameters is shown. A small change of iron stereochemistry leads to a small change of the iron electronic structure which could be detected by small changes of quadrupole splitting. It is expected that quadrupole splitting of iron gives new information for biomedical research on a molecular level.
	Reference	Z. Naturforsch. 51a, 381—388 (1996); received October 20 1995
	Published	1996
	Keywords	Mössbauer effect, Biomedical research, Quadrupole splitting, Iron electronic structure, Hemoglobin, Molecular diseases
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	TEI-XML for	default:Reihe_A/51/ZNA-1996-51a-0381.pdf
	Identifier	ZNA-1996-51a-0381
	Volume	51