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'Primary Structure' in keywords

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1	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

2	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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	Identifier	ZNB-1988-43b-1341
	Volume	43

3	Author	G.Erhard Braunitzer, Jone Liberatori, Hans-Jürgen Kolde	Requires cookie*
	Title	T he Primary Structure o f the /?-Lactoglobulin o f the W aterbuffalo (Bubalus arnee) A bteilung Proteinche mie, D-8033 Martinsried bei M ünchen and Centro Studio Alim entazione Animali in Produzione Zootecnica del CNR, III Reparto
	Abstract	The com plete amino acid sequence o f the /M actoglobu-line o f the waterbuffalo (Bubalus arnee) was established. The sequence o f peptides obtained by cleavage with BNPS-Skatole, CNBr and trypsin were determ ined autom atically by the help o f the sequenator. Only two differences were found in the ß-lactoglobulin o f the waterbuffalo compared with the bovine /M actoglobulin B.
	Reference	Z. Naturforsch. 34c, 880—881 (1979); received May 16 1979
	Published	1979
	Keywords	Milk, ß-Lactoglobulin, WaterbulTalo, Primary Structure
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	TEI-XML for	default:Reihe_C/34/ZNC-1979-34c-0880_n.pdf
	Identifier	ZNC-1979-34c-0880_n
	Volume	34

4	Author	Wolfgang Steer, G.Erhard Braunitzer	Requires cookie*
	Title	Chironomus thummi thummi (Insecta Diptera) The Sequence of a Dimeric Hemoglobin (Erythro cruorin), Com ponent IX, from Chironomus thummi thummi (Insecta Diptera)
	Abstract	The primary structure o f the dimeric hemoglobin (erythro cruorin) CTT-IX from the insect larva Chironomus thummi thummi (Insecta Diptera) is given. The sequence was deter mined automatically. The primary structure is compared with human a-chains.
	Reference	Z. Naturforsch. 34c, 882—884 (1979); eingegangen am 16. Mai 1979
	Published	1979
	Keywords	Dimeric Hem oglobin, Primary Structure, Insects
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	Identifier	ZNC-1979-34c-0882_n
	Volume	34

5	Author	Aftab Ahmed, Meeno Jahan, Gerhard Braunitzer, Helmut Pechlaner	Requires cookie*
	Title	(Mustela putorius, Mustelidae) Hemoglobins
	Abstract	The com plete am ino acid sequences o f the hem oglobins from the adult European polecat (Mustela putorius) are presented. The erythrocytes contain two hem oglobin com ponents and three globin chains (a I . a l l and ß). The primary structure of globin chains and o f the tryptic peptides determ ined in liquid-and gas-phase sequantors. Comparing the sequences o f the globin chains o f the polecat with that o f human H b -A , 17 (23.9%) substitutions were recognized in the a l , 16 (22.5%) in the a l l and 14 (20.4%) in the ß chain. A high degree o f hom ology observed with other representatives of the family M ustelidae.
	Reference	Z. Naturforsch. 44b, 817—8 (1989); received D ecem ber 22 1988
	Published	1989
	Keywords	European Polecat, Carnivora, H em oglobin, Primary Structure, Evolution
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	TEI-XML for	default:Reihe_B/44/ZNB-1989-44b-0817.pdf
	Identifier	ZNB-1989-44b-0817
	Volume	44

6	Author	Aftab Ahmed, M. Eeno, Jahan, G.Erhard Braumtzer	Requires cookie*
	Title	Carnivora: The Amino Acid Sequence of the Adult European Mink (Mustela lutreola, Mustelidae) Hemoglobins
	Abstract	The com plete am ino acid sequences o f the hemoglobins from the adult European mink (M ustela lutreola) are presented. The erythrocytes contain two hem oglobin com ponents and three globin chains. The isolation o f globin chains achieved by ion-exchange chromatography on a colum n o f C M -cellulose in 8 m urea buffer. The primary structure o f globin chains and o f the tryptic peptides determined in liquid-and gas-phase sequenators. The alignment o f the a-and ß-chains with those o f reported sequences from other carnivora species belonging to the family M ustelidae may give an insight into the evolution o f this molecule.
	Reference	Z. Naturforsch. 45c, 223 (1990); received July 18/October 31 1989
	Published	1990
	Keywords	European Mink, Carnivora, Hem oglobin, Primary Structure, H om ology
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	TEI-XML for	default:Reihe_C/45/ZNC-1990-45c-0223.pdf
	Identifier	ZNC-1990-45c-0223
	Volume	45