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Biomedical subjects

F Grimm

Publications and source records attributed to F Grimm.

17 recordsLinked to original sources
PubMed1991

Promastigote infectivity in Leishmania infantum.

Different clones and subpopulations of clones of Leishmania infantum were analyzed for their infective potential in vitro. Infectivity for macrophage-like cells (P388D1) and the response to a challenge with normal human serum enabled a clear differentiation between infective and non/low-infective populations. The results were confirmed by determination of parasite burdens in the spleens of infected golden hamsters. Long-term cultivation assays in vitro were used to test the influence of different cultivation conditions on the infectivity of promastigotes. An originally infective clone (LEM 768-A/ST) lost its infectivity during these assays but could regain it after the cultivation conditions had been changed. In addition, an originally non/low-infective clone (LEM 287-D/ST) could be forced to produce highly infective promastigotes. Infective cells were found only among stationary-phase promastigotes, i.e. after the cultures had reached a maximal number of cells per milliliter and the cell volume had clearly decreased.

Animals↗
PubMed1989

[The determination of blood parameters by Reflotron].

In this paper, the practicability of a quick diagnostic laboratory test to perform blood analysis in healthy pigeons was tested. The Reflotron manufactured by Boehringer Mannheim, works on a dry chemical basis, consists of a reflectance photometer and the accompanying test strips, is easy to use, and yields the result of the desired parameter in a maximum of three minutes. As test material plasma and serum were used. At the time the equipment was tested, test strips for glucose, cholesterol, hemoglobin, triglycerides, urea, uric acid, GOT, GPT and G-GT were available on the market. The usual laboratory "wet chemical" analysis procedures were used to compare the results. The obtained measurements were analyzed using describing and concluding statistics. The influence of gender, feed and time of day on the nine parameters was also considered.

Alanine Transaminase↗
PubMed1989

[The removal of foreign bodies in different birds].

Following problems are shown using slides: --ingrown rings and their removal with follow-up treatment, --the removal of fishhooks, especially in swans, --the removal of projectiles from the bird's body, --the removal of lead slivers from the digestive tract of parrots as well as the follow-up treatment, --the removal of gold chains, plastic tubing and other "toys" from the intestine. Gastrotomy in the parrot is described.

Animals↗
PubMed1989

[The use of collagen fasciae and fibrin adhesive for supporting wound healing in skin defects with large surfaces].

In 50 domestic pigeons, two circular pieces were removed from the skin to the right and left of the crista sterni, and the wounds were treated in different ways: A. with a collagen membrane dampened with a sodium chloride solution, B. with a fibrin glue, C. with a combination of A) and B). The wounds of group D were left untreated. Scab formation could be seen in all cases, also under the transparent membrane. The collagen membrane had no protective function in the experiment, however, it contributed to the acceleration of re-epithelialisation and the reduction of the wound diameter. The additional application of fibrin glue improved wound healing even further.

Animals↗
PubMed1989

[Dexamethasone and prednisolone use in pigeons].

The concentrations of dexamethasone and prednisolone in the plasma of pigeons are measured by radioimmunoassay. The plasma curves show a more rapid ascent and steeper descent after dexamethasone injection (1 mg, 2 mg, 4 mg and 10 mg/kg of body weight IM) than after prednisolone injection (3 mg, 5 mg, 10 mg and 50 mg/kg of body weight IM). The longer-lasting effect after prednisolone injection could likewise be seen in the white blood count. The immunosuppressive effect of glucocorticoid preparations especially should be considered when applying antibiotics.

Animals↗
PubMed1988

The primary structure of the hemoglobin of the Rock-Hopper penguin (Eudyptes crestatus, Sphenisciformes).

The blood of the Rock-Hopper Penguin contains only one hemoglobin component, corresponding to the Hb A of other birds. The primary structures of the alpha- and beta-chains are presented. The chains were separated by high-performance liquid chromatography and cleaved either enzymatically (alpha) or both enzymatically and chemically (beta). Both the native chains and their peptides were sequenced using liquid and gas phase sequenators. The peptides were aligned using their homology to the sequence of human hemoglobin and other bird hemoglobins. As compared to human hemoglobin, 44 amino-acid replacements are found in the alpha-chains (68% homology) and 47 in the beta-chains (67.8% homology). These exchanges involve seven alpha 1/beta 1 and one alpha 1/beta 2 contact in the alpha-chains, whereas in the beta-chains eight alpha 1/beta 1, one alpha 1/beta 2 and one hem contact are substituted. The influence of these replacements on the structure-function relationships in hemoglobin, as well as their importance for the diving ability of penguins, are discussed.

Amino Acid Sequence↗
PubMed1988

The primary structure of the hemoglobin of the Cormorant (Phalacrocorax carbo, Pelecaniformes).

The erythrocytes of the adult Cormorant contain two hemoglobin components in a ratio of 83% Hb A to 17% Hb D. The primary structures of the alpha A-, alpha D- and beta-chains are presented. The globin chains were separated by high-performance liquid chromatography and cleaved enzymatically and/or chemically. The native chains and their fragments were sequenced using liquid- or gas-phase sequencers, and the peptides aligned using the homology to human and to avian hemoglobin sequences. Compared to human hemoglobin, there are 46 amino-acid replacements in the alpha A-chains (67.4% homology), 65 replacements in the alpha D-chains (53.9% homology) and 45 replacements in the beta-chains (69.2% homology). In the functionally important regions, the percentage of amino-acid substitutions, as compared to human hemoglobin, is 13.2% in the alpha A-, 19.0% in the alpha D - and 16.0% in the beta-chains. The importance of the replacement beta 135 arginine (other birds)----glycine (Cormorant) in the phosphate-binding pocket and its effect on phosphate binding will be discussed.

Amino Acid Sequence↗
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

[Anesthesia in birds].

Anaesthesia in birds is ordered by law and is also necessary for various operations and manipulations. Anaesthesia by injection of Ketamin, which in special cases may be combined with Diazepam, has been found useful. Anaesthesia by inhalation with Halothan, Methoxyfluran or Isofluran is the most careful method. Local anaesthesia has few indications.

Anesthesia↗
PubMed1985

[Hemoglobin of tree sparrows (Passer montanus, Passeriformes): Sequence of the major (Hb A) and minor (Hb D) components].

Blood of the adult Tree Sparrow (Passer montanus) contains two hemoglobin components, Hb A (ca. 85%), Hb D (ca. 15%). They differ in their alpha-chains (alpha A, alpha D), the beta-chains are identical. The complete primary structures of alpha A-, alpha D- and beta-chains are presented. Comparison with the Greylag Goose (Anser anser) hemoglobin (Hb A) showed that the alpha A-chains differ by 22 amino-acid exchanges, the beta-chains by 16. Comparison with the minor component of the Pheasant (Phasianus colchicus colchicus) hemoglobin (Hb D) showed that the alpha D-chains differ by 34 amino-acid exchanges. Proline is found incorporated in an internal position of an alpha-helix (pos. 124, H7). In comparison to that of the Starling (Sturnus vulgaris) the ratio of amino-acid exchanges for beta: alpha A: alpha D chains is 1 : 7 : 4; in comparison to other birds this ratio is found to be 1 : 2 (1.4-2.2):3 (2.2-4).

Amino Acid Sequence↗
PubMed1985

[The hemoglobin of adult Andean condors (Vultur gryphus, Cathartiformes). The amino acid sequence of the major (HbA) and minor component (HbD)].

The complete amino-acid sequence of the alpha A- and the beta-chains of the major component (HbA) and the alpha D- and the beta-chains of the minor component (HbD) of Andean Condor (Vultur gryphus) is presented. The minor component with the alpha D-chains is present in smaller amounts (17%) than in other birds (25%). The comparison with the corresponding chains of Greylag Goose (Anser anser) shows 17 different amino acids (17 nucleotides, only one-point mutations) in the alpha A-chains and 8 (8 nucleotides) in the beta-chains. The alpha D-chains differ from those of the pheasant (Phasanius cholchicus cholchicus) in 24 amino acids (27 nucl., 3 two-point mutations). Seven alpha 1 beta 1-, one alpha 1 beta 2-, three alpha 1 alpha 1-contacts and one beta 1 beta 1-contact are exchanged. The systematy of Cathartiformes, Ciconiiformes and Phoenicopteriformes is discussed, based on the amino-acid exchanges of all known adult hemoglobins of birds.

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↗