Biomedical subjects

G Braunitzer

Publications and source records attributed to G Braunitzer.

At least 73 records · Page 4Linked to original sources

PubMed1988

The primary structure of the mandrill (Mandrillus sphinx, Primates) hemoglobin.

The complete primary structure of the hemoglobin from the Mandrill (Mandrillus sphinx, Primates) is presented. This hemoglobin comprises two components in approximately equal amounts (HB I and Hb II). The alpha-chains differ in positions 5 (A3) and 9 (A7) having Ala and Asn in the alpha I-chains and Asp and His in the alpha II-chains. The beta-chains are identical. The components could be separated by DEAE-Sephacel chromatography. The globin chains were obtained by carboxymethylcellulose chromatography or high-performance liquid chromatography. The sequences were established by automatic liquid or gas phase Edman degradation of the chains and their tryptic peptides. The alpha-chains show 9 and 11 and the beta-chains 8 exchanges compared with the corresponding human chains, respectively. In the beta-chains one alpha 1/beta 1- and one alpha 1/beta 2-contact is substituted. A comparison of the primary structures of the Mandrill hemoglobin chains with those of other species of the Cercopithecidae family shows that Mandrillus sphinx should be placed between Cercopithecus and Macaca on one side and Papio, Theropithecus and Cercocebus on the other.

Amino Acid Sequence↗

PubMed1988

High altitude and hemoglobin function in the vultures Gyps rueppellii and Aegypius monachus.

Functional characteristics of the stripped composite hemoglobins (Hbs) of the vultures Gyps rueppellii and Aegypius monachus that can fly at extremely high altitudes, and of component Hbs of G. rueppellii are reported, in relation to influences of pH, temperature and inositol hexaphosphate. G. rueppellii Hbs A, A' and D represent a sequence of increasing oxygen affinity, which is opposite to earlier results on avian Hb components, but correlates with two alpha-chain substitutions that predictably affect oxygen affinity. The homo- and heterotropic interactions in oxygen binding are related to primary structures of the constituent polypeptide chains to trace molecular adaptations to high-altitude respiration, and to physiological factors (pulmonary hypoxia and hypocapnia, body temperature shifts, and lung and nasal gas and heat exchange) to discern their possible survival value at altitudes of 11,300 m.

Acclimatization↗

PubMed1987

Embryonic pig hemoglobins Gower I (zeta 2 epsilon 2), Gower II (alpha 2 epsilon 2), Heide I (zeta 2 theta 2) and Heide II (alpha 2 theta 2): oxygen-binding functions related to structure and embryonic oxygen supply.

The common pig lacks a fetal hemoglobin but has four embryonic hemoglobins: Gower I (zeta 2 epsilon 2), Gower II (alpha 2 epsilon 2), Heide I (zeta 2 theta 2) and Heide II (alpha 2 theta 2) as well as adult Hb A (alpha 2 beta 2) and the amino acid sequence for each of the five constituent polypeptide chains has been established. The oxygenation characteristics of the five components, measured in relation to pH, temperature and the erythrocytic ligand 2,3-diphosphoglycerate (DPG), together with the changes in their relative concentrations during early embryonic life, are given. The findings indicate a progressive decrease in maternal-fetal oxygen affinity difference and thus in oxygen transfer efficacy at a given diffusion gradient that correlates with the development of the gas exchange structures. The functional properties of the individual hemoglobins are additionally discussed in relation to molecular structure.

2,3-Diphosphoglycerate↗

PubMed1987

High altitude respiration of birds. The primary structures of the major and minor hemoglobin component of adult European black vulture (Aegypius monachus, Aegypiinae).

The primary structures of the hemoglobin components Hb A and Hb D of the European Black Vulture (Aegypius monachus) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides in liquid phase and gas-phase sequenators. The sequences are compared with those of the Golden Eagle, and with those of the Andean Condor, a New World vulture. The possible evolutionary significance of the alpha D-chains is considered. This paper serves as a reference study for high-altitude respiration of Falconiformes.

Amino Acid Sequence↗

PubMed1987

Primary structure of the minor haemoglobins from the sea lamprey (Petromyzon marinus, Cyclostomata).

Erythrocytes of the adult Sea Lamprey Petromyzon marinus contain several haemoglobin species, but only the main constituent has hitherto been sequenced. The present paper describes the determination of the primary structures of the two minor species, whose electrophoretic mobilities are higher and lower than that of the main component. Tryptic peptides from both chains were purified by high-performance liquid chromatography, then sequenced and aligned by homology with the main haemoglobin. The fast and the major components appeared to be very similar, differing in only four positions (pos. 5: Ser----Thr; pos. 33: Thr----Ser; pos. 86: Val----Ala; pos. 99: Gly----Arg). The slow haemoglobin component, however, differed from the main component with respect to 27 amino-acid residues. The position of the three globins of Petromyzon marinus in the phylogenetic tree of haemoglobins is discussed and a relationship with primitive alpha-chains is postulated.

Amino Acid Sequence↗

PubMed1987

Chemistry of gas-phase sequencing: alternative bases.

The currently used base for gas-phase sequencing, trimethylamine, can be substituted by more hydrophobic tertiary amines without any problems. We used mainly N,N-dimethylallylamine and 3-(dimethylamino)propyne, both as aqueous solutions at constant temperature (40 degrees C). The advantages of these bases, which are liquids at room temperature, are their easy to regulate dosage, better stability and easier method of purification. The results of degradation with these bases are comparable with those obtained with trimethylamine.

Alkynes↗

PubMed1987

The primary structure of the hemoglobin from the bat Macrotus californicus (Chiroptera).

The complete primary structure of the hemoglobin from the bat Macrotus californicus (Chiroptera) is presented. This hemoglobin consists of only one component. The alpha- and beta-chains were separated by reverse phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation of the chains and the tryptic peptides, as well as of the C-terminal peptide obtained by acidic hydrolysis of the Asp-Pro bond in the beta-chains using the film- and gas-phase method. The sequences are compared with human hemoglobin: 15 amino-acid substitutions are found in the alpha- and 22 in the beta-chains. A comparison with the hemoglobin of Rousettus aegyptiacus and Myotis velifer shows a closer relation to the Mega- than to the Microchiroptera.

Amino Acid Sequence↗

PubMed1987

Molecular basis for ATP/2,3-bisphosphoglycerate control switch-over (poikilotherm/homeotherm) an intermediate amino-acid sequence in the hemoglobin of the great Indian rhinoceros (Rhinoceros unicornis, Perissodactyla).

The complete primary structure of the two hemoglobin components of the Great Indian Rhinoceros (Rhinoceros unicornis) is presented. The ratio for the two components B(alpha 2 beta I2): A(alpha 2 beta II2) is 6:4. Polypeptide subunits were separated by chromatography on CM-cellulose in a buffer containing 8M urea. The sequence was studied by degradation of the tryptic and hydrolytic cleavage products in a liquid phase sequencer. At position beta NA2 component B has Asp, whereas component A has Glu, an ATP-binding site in fish and reptilian hemoglobins. The other phosphate binding sites i.e. beta NA1 Val, beta EF6 Lys and beta H21 His are identical with 2,3-bisphosphoglycerate-(DPG)binding sites in mammalian hemoglobins, whereby rhinoceros hemoglobin resembles both ATP-sensitive poikilotherm hemoglobin and DPG-sensitive mammalian hemoglobin. The two components (beta I/beta II) additionally differ by exchange of Glu----Gly at position beta A3 and Gln----Lys at position beta GH3. The significance of these changes is discussed. Oxygenation properties of the two hemoglobins components and their dependence on ATP and DPG are given. The structure and function of Rhinoceros hemoglobin may give an insight into the evolution of the organic phosphate binding in vertebrate hemoglobins.

2,3-Diphosphoglycerate↗

PubMed1987

High-altitude respiration of birds. The primary structures of the major and minor hemoglobin component of adult goshawk (Accipiter gentilis, Accipitrinae).

The primary structures of the hemoglobin components Hb A and Hb D of the adult Goshawk (Accipiter gentilis) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. Component separation was achieved by FPLC-chromatography on a TSK SP-5PW column in phosphate-buffers with a linear gradient of NaCl. The amino-acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-phase and gas-phase sequenators. The sequences are aligned with those of European Black Vulture (Aegypius monachus). Phylogenetic aspects and physiological properties for Goshawk hemoglobin are inferred from sequence data. A detailed evaluation of the oxygen-binding properties has been carried out during a prolonged study of the noteworthy ability of Falconiformes to cope with extremely low oxygen partial pressures, and will be the subject of a forthcoming paper.

Altitude↗

PubMed1987

Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).

The amino-acid sequence of phospholipase A2 from the neurotoxin vipoxin of the Bulgarian Viper (Vipera ammodytes ammodytes, Serpentes) is presented. The enzyme consists of 122 amino-acid residues including 7 disulfide bonds and thus belongs to phospholipases A2 group IIA. The sequence was determined by automatic Edman degradation of the intact chain and of the peptides obtained after tryptic hydrolysis of the oxidized chain. The short cleavage time of 30 min and another limited tryptic digestion of the oxidized and citraconylated chain provided overlapping peptides. Sequencing was done with liquid- and gas-phase sequenators. The complete alignment of all peptides was facilitated by the high degree of homology with known viperid venom phospholipases A2. In common with mammalian phospholipases, the tryptophan residue in position 30 (essential for enzymatic activity) as well as the histidine in position 47 in the active site are present. Vipoxin phospholipase A2 shows 53.3% homology with another phospholipase A2 from Vipera ammodytes ammodytes venom (Ammodytoxin B), whereas 62% homology was found between both subunits of vipoxin phospholipase A2 and its inhibitor. This high degree of identity can be accounted for in terms of a common origin by gene duplication.

Amino Acid Sequence↗

PubMed1987

The primary structure of the hemoglobin of Malayan sun bear (Helarctos malayanus, Carnivora) and structural comparison to other hemoglobin sequences.

The complete primary structure of the alpha- and beta-chains of the hemoglobin of Malayan Sun Bear (Helarctos malayanus) is presented. After cleavage of the heme-protein link and chain separation by RP-HPLC, amino-acid sequences were determined by Edman degradation in liquid- and gas-phase sequenators. An interesting result of this work is the demonstration that the hemoglobin of Malayan Sun Bear is identical to the hemoglobins of Polar Bear (Ursus maritimus) and Asiatic Black Bear (Ursus tibetanus). The paper gives an updated table of identical hemoglobin chains from different species. This paper may be considered as a compilation of work on the genetic relationship of Pandas.

Amino Acid Sequence↗

PubMed1987

The primary structure of the hemoglobin of an Indian flying fox (Cynopterus sphinx, Megachiroptera).

The hemoglobin of the Indian flying fox Cynopterus sphinx contains only one component. In this work, we are presenting its primary structure. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas-phase Edman degradation of the chains and their tryptic peptides, as well as of the peptide obtained by acid hydrolysis of the Asp-Pro bond in the beta-chains. The alpha-chains show 14 and the beta-chains 19 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains one amino-acid exchange involves an alpha 1/beta 1 contact. In the beta-chains one heme contact, three alpha 1/beta 1- and one alpha 1/beta 2-contacts are exchanged. The functional and evolutionary aspects of these findings are discussed.

Amino Acid Sequence↗

PubMed1987

Primary structure and functional properties of the hemoglobin from the free-tailed bat Tadarida brasiliensis (Chiroptera). Small effect of carbon dioxide on oxygen affinity.

The hemoglobin of the Free-Tailed Bat Tadarida brasiliensis (Microchiroptera) comprises two components (Hb I and Hb II) in nearly equal amounts. Both hemoglobins have identical beta-chains, whereas the alpha-chains differ in having glycine (Hb I) or aspartic acid (Hb II) in position 115 (GH3). The components could be isolated by DEAE-Sephacel chromatography and separated into the globin chains by chromatography on carboxymethyl-cellulose CM-52. The sequences have been determined by Edman degradation with the film technique or the gas phase method (the alpha I-chains with the latter method only), using the native chains and tryptic peptides, as well as the C-terminal prolyl-peptide obtained by acid hydrolysis of the Asp-Pro bond in the beta-chains. The comparison with human hemoglobin showed 18 substitutions in the alpha-chains and 24 in the beta-chains. In the alpha-chains one amino-acid exchange involves an alpha 1/beta 1-contact. In the beta-chains one heme contact, three alpha 1/beta 1- and one alpha 1/beta 2-contacts are substituted. A comparison with other chiropteran hemoglobin sequences shows similar distances to Micro- and Megachiroptera. The oxygenation characteristics of the composite hemolysate and the two components, measured in relation to pH, Cl-, and 2,3-bis-phosphoglycerate, are described. The effect of carbon dioxide on oxygen affinity is considerably smaller than that observed in human hemoglobin, which might be an adaptation to life under hypercapnic conditions.

Amino Acid Sequence↗

PubMed1987

N-terminal amino-acid sequence of a sphingolipid activator protein missing in a new human Gaucher disease variant.

A naturally occurring non-enzymic sphingolipid activator protein (A1a activator) shown previously to be immunochemically not detectable in a new variant of human Gaucher disease (glucosylceramide-lipidosis) without glucosylceramidase deficiency was characterized by partial sequence analysis. The N-terminal amino-acid sequence of the A1a activator--a glycoprotein with high carbohydrate content--could be determined up to position 38. About 20% of the polypeptide chain are shorter by two amino-acid residues at the N-terminal end. Position 22 seems to be occupied by a carbohydrate-binding asparagine. The N-terminus of the A1a activator does not show any homology with the activator for the enzymic sulfatide degradation.

Amino Acid Sequence↗

PubMed1987

The primary structure of the pallid bat (Antrozous pallidus, Chiroptera) hemoglobin.

The complete primary structure of the hemoglobin from the Pallid Bat (Antrozous pallidus, Microchiroptera) is presented. This hemoglobin consists of two components with identical amino-acid sequences, differing, however, in the N-terminus which is formylated in 12.5% of the beta-chains. The alpha- and beta-chains were separated by reversed phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation with the film technique or gas phase method using the native chains and the tryptic peptides. The formylation of a part of the N-terminal peptide of the beta-chains was determined by mass spectrometric examination. Compared to the corresponding human chains we found 14 substitutions in the alpha-chains and 21 in the beta-chains. One substitution in the alpha-chains and three in the beta-chains are involved in alpha 1/beta 1-contacts. Among these the exchange beta 123(H1)Thr----Cys is unusual because cysteine was so far not found in this position of mammalian beta-chains. Compared to the hemoglobin of Myotis velifer, another representative of the family Vespertilionidae, 5 residues are replaced in the alpha-chains and 18 in the beta-chains.

Amino Acid Sequence↗

PubMed1987

The primary structure of the hemoglobins of the adult jaguar (Panthera onco, Carnivora).

The primary structure of the hemoglobins from Jaguar (Panthera onco) are presented. Electrophoretic separations without and with a dissociating agent revealed the presence of two hemoglobin components, alpha 2 beta I2 and alpha 2 beta II2. The separation of the hemoglobin components was achieved by ion-exchange chromatography. The globin chains were separated by ion-exchange chromatography and also by reversed phase HPLC. The amino-acid sequences of the native chains and peptides were determined by liquid-phase and gas-phase sequencing. N-Acetylserine was detected by FAB-mass spectroscopy as N-terminal group of the beta I chain. The sequences are compared with that of human hemoglobin (Hb A).

Amino Acid Sequence↗

PubMed1987

Preparation and characterization of N epsilon-(2,3-dihydroxypropyl)-L-lysine and its phenylthiohydantoin derivative.

Convenient methods for preparative synthesis of N epsilon-(2,3-dihydroxypropyl)-L-lysine and its phenylthiohydantoin derivative are described. The former compound was characterized by elemental analysis, melting point, and ion-exchange chromatography and the latter by elemental analysis, melting point, UV-spectrum, HPLC and thin-layer chromatography. This study was performed for investigations of lysine residues in proteins.

Amino Acids↗

PubMed1987

The primary structures of the major and minor hemoglobin-components of adult Andean goose (Chloephaga melanoptera, Anatidae): the mutation Leu----Ser in position 55 of the beta-chains.

The primary structures of the hemoglobin components Hb A and Hb D of the adult Andean Goose (Chloephaga melanoptera) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the globin chains and of the tryptic peptides in liquid- and gas-phase sequenators. The sequences are aligned with those of Greylag Goose (Anser anser) as a biological reference and other sequences of birds. A detailed evaluation of all residues of Andean Goose hemoglobins on the basis of the 12000 known avian globin sequences leads to a molecular pattern for high-altitude respiration of geese. The replacement of functional and structural importance is the unique occurrence of the residue beta 55 Leu----Ser (all other exchanges are functionally neutral), interrupting the same alpha 1 beta 1-interface contact (alpha 119-beta 55) that accounts for high-altitude respiration of the Barheaded Goose (Anser indicus); there the mutation is found on alpha A 119. Loosening the constraints of this interface must be interpreted as a destabilization of the low-affinity T-structure in favour of the high-affinity R-structure. The structural and functional significance of this interface for the molecular biology of high-altitude respiration of the Andean Goose and Barheaded Goose is discussed. Since Hb A consists of alpha A2 beta 2 and Hb D consists of alpha D2 beta 2 the mutation occurring in blood of the Andean Goose affects both hemoglobins whereas in the case of the Barheaded Goose only Hb A is affected. These results show that Hb D can be considered a biological reserve to enlarge situatively the normal hemoglobin function. A general molecular pattern for permanent (selective advantage of high intrinsic oxygen affinity) and transitory (selective advantage of graded oxygen affinities) adaptation to hypoxia is discussed. A survey on the sequence homology of the globin chains of geese (Anserinae) and ducks (Anatinae) is given.

Altitude↗