PubMed Health⌕ Search

Biomedical subjects

H Wiesner

Publications and source records attributed to H Wiesner.

At least 37 records · Page 2Linked to original sources
PubMed1986

An evolutionary conserved early replicating segment on the sex chromosomes of man and the great apes.

Replication studies on prometaphase chromosomes of man, the chimpanzee, the pygmy chimpanzee, the gorilla, and the orangutan reveal great interspecific homologies between the autosomes. The early replicating X chromosomes clearly show a high degree of conservation of both the pattern and the time course of replication. An early replicating segment on the short arm of the X chromosomes of man (Xp22.3) which escapes inactivation can be found on the X chromosomes of the great apes as well. Furthermore, the most early replicating segment on the Y chromosomes of all species tested appears to be homologous to this segment on the X chromosomes. Therefore, these early replicating segments in the great apes may correspond to the pseudoautosomal segment proposed to exist in man. From further cytogenetic characterization of the Y chromosomes it is evident that structural alterations have resulted in an extreme divergence in both the euchromatic and heterochromatic parts. It is assumed, therefore, that, in contrast to the X chromosomes, the Y chromosomes have undergone a rapid evolution within the higher primates.

Animals↗
PubMed1986

[Intrinsic oxygen affinity of hemoglobins: the hemoglobin of bisons (Bison bonasus,Bovidae)].

The hemoglobin from a European Bison (Bison bonasus) was analysed and the complete primary structures of the alpha I-, alpha II-and beta-chains have been determined. The alpha I- and alpha II-chains differ only at position alpha 19 (Asp----Gly). The beta-chains are homogeneous. The sequences are compared with the globin chains of Bison bison and bovine and the polymorphism of the alpha-chains is discussed. On the basis of the primary structure it may be concluded that the hemoglobin of Bison bonasus belongs to the group of hemoglobins with intrinsically low oxygen affinity.

Amino Acid Sequence↗
PubMed1985

Primary structure of the hemoglobins from the greater Kudu antelope (Tragelaphus strepsiceros).

The adult greater Kudu antelope has two hemoglobin components, Hb A and Hb B, with one alpha and two beta chains. The complete amino-acid sequences of these three chains are presented. The two beta chains differ only in one residue at position 16 (Gly----Ser) and may be the product of two allelic genes. The primary structure of the chains was determined by sequencing the tryptic peptides after their isolation from the tryptic digest of the chains by high performance liquid chromatography. The alignment of these peptides was deduced from homology with the chains of bovine hemoglobin. Between the Kudu hemoglobins and those of cattle a high degree of homology was found.

Amino Acid Sequence↗
PubMed1985

Studies on yak hemoglobin (Bos grunniens, Bovidae): structural basis for high intrinsic oxygen affinity?

Two types of alpha- and two types of beta-chains are found in the hemoglobin of yak population. The complete amino-acid sequences of the four polypeptide chains were determined. The two alpha-chains differ by two and the two beta-chains by three amino-acid substitutions. The substitution of valine at position 135 in the beta II-chain may be responsible for the high intrinsic oxygen affinity of yak hemoglobin.

Amino Acid Sequence↗
PubMed1985

[Practical advice concerning the immobilization of wild and zoo animals].

The usage of ketamine, etorphine and carfentanyl, each combined with xylazine, for the immobilization of captive and free living wild animals is reported. The side-effects of these immobilizaion combinations are discussed. The dosage rates of the immobilization combinations for mammmals, birds and reptiles are presented in tabular form.

Acepromazine↗
PubMed1984

Phosphate-haemoglobin interaction. The primary structure of the haemoglobin of the African elephant (Loxodonta africana, Proboscidea): asparagine in position 2 of the beta-chain.

The primary structure of the haemoglobin of the African Elephant (Loxodonta africana) is reported. The sequence was determined by means of a sequenator. The haemoglobin differs in 26 amino acids in the alpha-chains and in 27 in the beta-chains from that of adult human haemoglobin. The haemoglobin of the African Elephant, like that of the Indian Elephant and Ilama, has only 5 binding sites for polyphosphate. This finding explains the low p(O2)50 value in whole blood as a result of the lower 2,3-bisphosphoglycerate-haemoglobin interaction. This is discussed in relation to aspects of respiratory physiology; some points are also of interest with regard to the Second Punic War and Hannibal's crossing of the Alps.

2,3-Diphosphoglycerate↗
PubMed1983

[Primary structure of alpha and beta chains from the major hemoglobin component of the magpie goose (Anseranas semipalmata, Anatidae)].

The amino acid sequence of the alpha and beta chains from the major hemoglobin component (HbA) of Australian Magpie Goose (Anseranas semipalmata) is given. The minor component with the alpha D chains was detected, but only found in low concentrations. By homologous comparison, Greylag Goose hemoglobin (Anser anser) and Australian Magpie Goose alpha chains differ by 13 amino acids or 17 nucleotide (4 two point mutations) exchanges, beta chains by 6 exchanges. Seven alpha 1 beta 1 contacts are modified by substitutions in positions alpha 30-(B11)Glu leads to Gln, alpha 34(B15)Thr leads to Gln, alpha 35(B16)-Ala leads to Thr, alpha 36(B17)Tyr leads to Phe, beta 55(D6)Leu leads to Ile, beta 119(GH2)Ala leads to Ser and beta 125(H3)Glu leads to Asp. Further, one alpha 1 beta 2 contact point was changed in beta 39(C5)Gln leads to Glu. Mutation in this position, except in two abnormal human hemoglobins, was not found in any species. Amino acid exchanges between hemoglobin of Australian Magpie Goose and other birds are discussed.

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↗
PubMed1979

Immobilisation of free-ranging Galapagos sea lions (Zalophus californianus wollebaeki).

Nine free-ranging Galápagos sea lions were immobilised for marking, using a combination of ketamine (3 to 5 mg per kg) and xylazine (0.5 to 1.0 mg per kg). The degree of effect depended largely on the animals' behavioural and physiological state before immobilisation (after parturition, high arousal, subject to aggression, etc.) All nine animals survived. Overheating in the immobilised state may quickly result in heart and circulatory failures.

Animals↗
PubMed1979

[High-dose methotrexate therapy in osteogenic sarcoma: plasma pharmakokinetics to predict toxicity (author's transl)].

In 22 patients with osteogenic sarcoma, treated with 103 high-dose methotrexate infusions (6-8.5 g/m2 in 4-6 h) plasma methotrexate levels were measured with a specific and rapid radioimmunoassay. Nontoxic infusions were associated with methotrexate concentrations below 8.0 X 10(-6) mol/l at 24 h, 8.0 X 10(-7) mol/l at 48 h and 4.25 X 10(-7)/mol/1 at 72 h. All patients with 48 h methotrexate levels above 1 X 10-6 mol/l manifested severe toxicity with myelosuppression and stomatitis due to delayed methotrexate excretion. Rise of serum creatinine was not reliable to predict oxicity. Determination of 48- and 72-h methotrexate concentrations proved to be a valuable method for identifying patients at high risk for toxic side effects. Additional citrovorum factor may thus be given in time.

Adolescent↗
PubMed1979

[Respiration at high altitudes, phosphate-protein interaction: the sequence of hemoglobins from guinea pig and dromedary (author's transl)].

The sequence of the main hemoglobin component of the guinea pig (Cavia aerea f. porcellus, Caviidae) and that of the hemoglobin of the dromedary (Camelus dromedarius, Camelidae) is given. The sequence is obtained automatically by the sequenator using the quadrol and the propyne programme. The sequence of the alpha-and beta-chains of the guinea pig is compared with that of the human hemoglobin; the sequence of the dromedary in comparison to the Ilama shows in the alpha-chains five amino acid exchanges, in the beta-chains there are only two exchanges in beta 2 and beta 76. Beta 2 in dromedary is the P2-glycerate contact histidine. This sustains the interpretation of the high altitude respiration of the Ilama as mutation beta2His leads to Asn.

Altitude↗
PubMed1975

[Whiplash injuries of the cervical spine. A catamnestic study].

Whiplash injuries of the cervical spine are due to the rapid sequence of movements in opposite direction. They are mainly following rear-end collisions where the trunk is pushed rapidly forward. Very important forces act therefore on the different segments of the cervical spine and lead to lesions of the perispinal soft tissues, of the ligaments, of the disks and the bony structures. In 24 tables, the signs and symptoms in 104 personal cases observed for a period which lasted more than 4 years are described. Amongst the clinical signs there are cervical strain, cervico brachial pain, headaches, radicular signs as well as symptoms of concussion and cercial medullar lesion. Radiological findings are discrete; functional X-rays sometimes show local diminution of motility in a single segment. The treatments, amongst these immobilisation and local heat, are discussed. The unusually long duration of local disturbance is stressed. Signs of neurasthenia are part of the typical findings and do not at all mean a secondary neurotic development.

Accidents, Traffic↗