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Biomedical subjects

G Braunitzer

Publications and source records attributed to G Braunitzer.

At least 145 records · Page 8Linked to original sources
PubMed1983

The amino-acid sequence of Northern Mallard (Anas platyrhynchos platyrhynchos) hemoglobin.

The complete amino-acid sequence of the major hemoglobin component (HbA) of the adult Northern Mallard (Anas platyrhynchos platyrhynchos) is presented. A minor component HbD was also detected but in low concentrations. The sequences of alpha A- and beta-chains were established by automatic Edman degradation on tryptic peptides and peptides obtained by specific chemical cleavages. The alignment of the peptides was performed by comparison with the alpha A- and beta-chains of Greylag Goose hemoglobin (Anser anser). Thereby an exchange of five positions in the alpha A-chains and three in the beta-chains was observed. No exchanges were found in the surroundings of the heme, in alpha 1 beta 2-contact points, or allosteric regulatory sites. In the alpha 1 beta 1-subunit interface one amino-acid residue in alpha A-chains and one in beta-chains are exchanged. By comparison with the amino-acid sequence derived from globin genes of Domestic Duck (Anas platyrhynchos), the alpha A-chains differ by two exchanges in the N-terminal region and the beta-chains by five exchanges the in C-terminal region. The comparison of the amino-acid sequence derived from alpha A-globin gene of the Moscovy Duck (Cairina moschata) and alpha A-chains of the Northern Mallard, shows only one replacement.

Amino Acid Sequence↗
PubMed1983

[Primary structure of subtilisin DY].

The complete amino-acid sequence of subtilisin DY, an extracellular alkaline proteinase produced by Bacillus subtilis, strain DY, is presented. The enzyme's primary structure was elucidated using peptides obtained by tryptic hydrolysis and peptides released from BrCN, tryptophan and Asn-Gly cleavage (using hydroxylamine). The peptides were isolated by gelfiltration and by reversed phase high performance liquid chromatography and were degradated automatically in the sequenator. The complete sequence has been verified by peptide overlapping. The subtilisin DY polypeptide chain, like that of subtilisin Carlsberg, consists of 274 amino-acid residues. 32 Amino-acid replacements were found between these two molecules (37 nucleotide mutations, 5 of them two-point mutations). Between the subtilisins DY and Novo 82 amino-acid residue replacements (106 nucleotide mutations, 24 two-point mutations) and one deletion were found. The polypeptide chains of the three subtilisins mentioned were compared and some differences discussed.

Amino Acid Sequence↗
PubMed1983

[Primary structure of hemoglobins of the musk rat (Ondatra zibethica, Rodentia)].

The amino-acid sequence for the hemoglobin of the musk-rat (Ondatra zibethica) was determined. The sequence of both chains was established by automatic Edman-Begg degradation of the tryptic peptides and, in the case of the beta-chains additionally of the prolyl-peptide. The complete primary structure of the alpha-chains differs at 22, that of the beta-chains at 36 positions from the adult human hemoglobin. There are no changes in the heme-binding residues, the alpha 1--beta 2 contact positions and the allosteric regulator sites. In the heme-pocket we found beta 44 Ser leads to His and 8 positions changed within the alpha 1--beta 1 contact regions. These changes are discussed with respect to the function of the respective regions.

Amino Acid Sequence↗
PubMed1983

[The primary structure of the alpha-amylase inhibitor Hoe 467A from Streptomyces tendae 4158. A new class of inhibitors].

The native or modified alpha-amylase inhibitor Hoe 467A - isolated from the culture medium of Streptomyces tendae 4158 - and overlapping peptides were degraded by the automatic Edman technique. The oxidized or aminoethylated or oxidized and maleoylated inhibitor was digested with trypsin and the native inhibitor with pepsin. Further digestion with Staphylococcus aureus proteinase was also carried out. After peptic digestion two cystin peptides were isolated, which allowed the establishment of the disulfide bonds. The alpha-amylase inhibitor is a polypeptid consisting of 74 amino-acid residues with a molecular mass of 7958 Da. The inhibitor is composed of all naturally occurring amino acids except methionine and phenylalanine and shows no sequence homology to known inhibitors. The clinical and pharmacological importance in respect to the inhibitors ability for inactivation of human salivary and pancreatic alpha-amylase is discussed. Especially the proteinase resistance of the inhibitor enables a clinical application in human (e.g. Diabetes mellitus) per os.

Amino Acid Sequence↗
PubMed1983

[Hemoglobin of the golden eagle (Aquila chrysaetos, Accipitriformes): amino acid sequence of the alpha A- and beta chains of the principal component].

The primary structures of the alpha A- and beta-chains from the major hemoglobin component of Golden Eagle (Aquila chrysaetos) are given. By homologous comparison, Greylag Goose (Anser anser) hemoglobin and Golden Eagle alpha A-chains differ by 17 amino acids or 19 nucleotides (2 two-point mutations), beta-chains by 9 exchanges. Five substitutions have modified alpha 1 beta 1-contacts, one substitution, one alpha 1 beta 2-contact and one alpha 1 alpha 1-contact. Differences by homologous comparison to other hemoglobins of birds are discussed.

Amino Acid Sequence↗
PubMed1983

[The primary structure of hemoglobins of the rock hyrax (Procavia habessinica, Hyracoidea): insertion of glutamine in the alpha chains].

The chromatography of the hemoglobin of the rock hyrax (Procavia habessinica) gives two components (73% HbI and 27% HbII). The amino-acid analysis and the sequences of the globin chains elucidated with the phenylthiohydantoin method, did not show any differences between the alpha I and alpha II or beta I and beta II chains, respectively. The different chromatographical behaviour cannot be explained. After chain separation by chromatography on CM-52 cellulose, all four primary structures were elucidated automatically in a sequenator on the chains and the tryptic peptides. In 20% of the beta I chains the N-terminal valine was blocked by acetyl. The alignment was performed by homology with the chains of human adult hemoglobin. The alpha chain of the rock hyrax has 142 amino-acid residues, i.e. one residue more than normal mammalian alpha chains, caused by an insertion of glutamine in the GH region supposed between positions 115 and 116. A comparison of human and hyrax hemoglobins shows an exchange of 21 amino-acid residues in the alpha chains and of 24 in the beta chains. Some substitutions in alpha 1 beta 1 contacts and in the surrounding of the heme are not supposed to effect the function of the hemoglobin. The phylogenetic relationship between the rock hyrax and the Indian elephant (Elephas maximus) on the one hand and with some Perissodactyla on the other, is discussed. Up to now the exchanges of alpha 110(G17)Ala leads to Ser and beta 56(D7)Gly leads to His have only been found in hyrax and elephant. This indicates a certain relationship between Hyracoidea and Proboscidea.

Amino Acid Sequence↗
PubMed1983

[The primary structure of hemoglobins from the bottlenosed dolphin (Tursiops truncatus, Cetacea)].

Only one hemoglobin component was found in the bottlenosed dolphin (Tursiops truncatus, Cetacea). The alpha and beta chains were separated by chromatography on CM-52 cellulose. The complete primary structures of both chains were established by automatic Edman degradation of the chains and the tryptic peptides. The alignment was done by homology with alpha und beta chains of adult human hemoglobin. A comparison of these two hemoglobins shows an exchange of 22 amino acid residues in the alpha chains and of 20 in the beta chains which corresponds to the phylogenetic distance between primates and cetacea. In the surroundings of the heme we found one substitution in the beta chains. In the alpha 1 beta 1 subunit interphase three and four residues are exchanged respectively in the alpha and beta chains. The possible influence of two exchanges in the alpha 1 beta 2 contact region (alpha 38 (C3) Thr leads to Ser and alpha 44 (CD2) Pro leads to Ser) on the oxygen affinity is discussed. Compared with hemoglobins of terrestrial mammals the primary structure of dolphin hemoglobin shows no amino acid substitutions, which alter the function of the molecule significantly. The adaptation to hypoxic conditions during diving is regulated by other mechanisms.

Amino Acid Sequence↗
PubMed1983

[Primary structures of the alpha and beta chains from the major hemoglobin component of the ostrich (Struthio camelus) and American rhea (Rhea americana) (Struthioformes). Aspects of respiratory physiology and taxonomy].

The primary structures of the alpha A- und beta-chains from the major hemoglobin component of the Ostrich (Struthio camelus) and American Rhea (Rhea americana) are given. The minor component with the alpha D-chains was detected in Ostrich in several concentrations, in American Rhea as in chicken and pheasant (about 40%). By homologous comparison, Greylag Goose (Anser anser) hemoglobin and Ostrich alpha A-chains differ by 15 amino acids or 16 nucleotide (1 two-point mutation) exchanges, beta-chains by 4 exchanges. Four substitutions modify alpha 1 beta 1-contacts and one phosphate contact. American Rhea and Greylag Goose hemoglobin alpha A-chains differ by 20 amino acids or 23 nucleotides (3 two-point mutations), beta-chains by 4 exchanges. Two substitutions modify alpha 1 beta 1-contacts, one phosphate contact and one heme contact. Oxygen affinity of three hemoglobin components of Ostrich are measured and the results are discussed. Systematic and evolution of Ostrich and American Rhea are discussed.

Amino Acid Sequence↗
PubMed1982

Hemoglobins, XLVIIII. The primary structure of a monomeric hemoglobin from the hagfish, Myxine glutinosa L.: evolutionary aspects and comparative studies of the function with special reference to the heme linkage.

Hagfish hemoglobin has three main components, one of which is Hb III. It is monomeric and consists of 148 amino acid residues (M = 17 350). Its complete primary structure, previously published, is discussed here. The proximal amino acid (F8) of the heme linkage is histidine as always in the hemoglobins, but the regularly expected distal histidine E7 is substituted by glutamine. This substitution, leading to a new kind of heme linkage, has hitherto only been demonstrated in opossum hemoglobin. It is suggested that E7, Gln, is directed out of the heme pocket, and that the adjacent Ell, Ile, is directed toward the inside of the pocket, giving the distal heme contact instead of histidine. Myxine Hb III has an additional tail of 9 amino acid residues at its N-terminal end, as has the hemoglobin of Lampetra fluviatilis. The genetic codes of Myxine and Lampetra hemoglobins show 117 differences, in spite of many morphological resemblances between hagfish and lamprey. Their primary hemoglobin structures show differences substantial enough to be compatible with the divergence of the two families some 400-500 million years ago.

Amino Acid Sequence↗
PubMed1982

Hemoglobins, XLV. The amino acid sequence of pheasant (Phasianus colchicus colchicus) hemoglobins.

Pheasant hemoglobin is heterogenous and contains two components: a major one called HbA (70% of total amount) and a minor one called HbD (25% of total amount). HbA contains alpha A-chain, while HbD contains alpha D-chain. The amino acid sequences of both hemoglobins are given. The sequences were determined by automatic Edman degradation of tryptic peptides and peptides obtained by specific chemical cleavages. Between alpha A- and alpha D-chains a large difference of 57 amino acids was found. The primary structures of beta-chains from both hemoglobins are identical. The alpha A-chains contain no tryptophan, only one methionine and two cysteines. The alpha D-chains contain one tryptophan, four methionines and one cysteine. By homologous comparison with greylag goose hemoglobin the alpha A-chains differ by 19 exchanges, beta-chains by 7 exchanges. The alpha D-chains differ by 10 exchanges in comparison to alpha D-chains from chicken hemoglobin D. In the alpha A-chains valine was found to position alpha 63 (E12) as was the case for alpha-chains of barheaded goose. In the alpha D-chains however leucine was found in this position.

Amino Acid Sequence↗
PubMed1982

[The sequence of hemoglobins from an asiatic wild ass and a mountain zebra].

The hemoglobins from an asiatic wild ass (Equus hemionus kulan) and a mountain zebra (Equus zebra) were analysed and the complete primary structure of the alpha and beta chains are described. The wild ass globin was separated in two alpha chains (alpha I and alpha II) and one beta-chain by means of chromatography on CM-cellulose in 8M urea buffer at pH 6.5. The wild ass globin shows polymorphism in the alpha-chain like the horse hemoglobin. Under the same chromatographic conditions only one alpha and one beta-chain were found in the zebra globin. The primary structures were determined with the aid of an automatic liquid phase sequenator. A comparison of the sequence data shows there is only one amino acid differing between the alpha I- and alpha II-chain of wild ass. In position 20 asparagine (apha I) is substituted for histidine (alpha II). There are three amino acid replacements between the alpha I-chain in wild ass and an alpha-chain in horse (alpha 24 Phe, alpha 60 Lys); alpha I20 Asn leads to His, alpha 23 Asp leads to Glu, alpha 131 Thr leads to Ser. Two amino acid substitutions were found between the alpha-chains in zebra and horse, alpha 20 Asn leads to His and alpha 131 Thr leads to Ser. The beta-chains of wild ass zebra hemoglobins are identical, but two amino acid differences were found between wild ass and horse globins, beta 52 Ala leads to Gly and beta 87 Gln leads to Ala.

Amino Acid Sequence↗
PubMed1982

The amino acid sequence of Canada goose (Branta canadensis) and mute swan (Cygnus olor) hemoglobins. Two different species with identical beta-chains.

The amino acid sequences of the alpha- and beta-chains from the major hemoglobin component (HbA) of Canada goose (Branta canadensis) and mute swan (Cygnus olor) are given. The alpha-chains are of the alpha A-type, since alpha D-type was expressed but only found in low concentrations. By homologous comparison, greylag goose hemoglobin (Anser anser) and Canada goose hemoglobin alpha-chains differ by two exchanges, and beta-chains by three exchanges. A valine substitution for threonine was found at position alpha 34 (B15). This exchange is a result of a two point mutation. Thus, there are three nucleotide mutations in alpha-chains, as in beta-chains. Substitutions in positions alpha 34 (B15) and beta 125 (H3) have modified intersubunit contacts (alpha 1 beta 1-contacts). A comparison of mute swan hemoglobin with greylag goose hemoglobin shows four exchanges in alpha-chains and three in beta-chains. Canada goose and mute swan have identical beta-chains, while alpha-chains differ in two amino acids. One of these exchanges is implicated in one of the alpha 1 beta 1-contact points (alpha 34) where isoleucine substitution for valine was found. Comparison of hemoglobins from different species in the same tribe (Anserini) shows a high homology between Canada goose and mute swan hemoglobins.

Amino Acid Sequence↗
PubMed1982

[Hemoglobins XLVI: the primary structure of the alpha-chain of armadillo (Dasypus novemcinctus, Edentata) hemoglobin (author's transl)].

The complete primary structure of the identical alpha-chains of the two hemoglobin components of armadillo (Dasypus novemcinctus) is presented. It was established on the tryptic peptides by automatic Edman degradation. The alignment was done according to the homology with human alpha-chains. 25 differences were found between both chains. A comparison of the functional amino acid residues shows one substitution in the surrounding of the heme, there in the alpha 1 beta 1 - and two in the alpha 1 beta 2 - subunit interface. The two replacements alpha 38(C3)Thr leads to Pro and alpha 44(CD) - Pro leads to Ser may contribute to the high oxygen affinity of the armadillo hemoglobin by destabilization of the T-structure.

Amino Acid Sequence↗