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T Kruse

Publications and source records attributed to T Kruse.

52 records · Page 3Linked to original sources
PubMed1985

Amino acid transport across the human blood-CSF barrier. An evaluation graph for amino acid concentrations in cerebrospinal fluid.

The correlation of cerebrospinal fluid (CSF)/serum concentration quotients was used as a method for identification of amino acids which are transported by a common carrier system across the blood-CSF barrier. Isoleucine, leucine, valine, phenylalanine, tyrosine and lysine were found to compete for the same carrier system. This group of amino acids in man was found to be different from the system described as a neutral amino acid carrier at the blood-brain barrier in rats. In man, methionine and tryptophan do not compete with the other neutral amino acids for the same carrier system. In contrast, lysine as a basic amino acid is found to be correlated with the same transport system as the five neutral amino acids. A graph for the evaluation of pathological amino acid concentrations in CSF is presented. Patients with a blood-CSF barrier dysfunction for proteins showed partly normal, partly increased, CSF/serum concentration quotients for the amino acids. Hydroxyproline could be identified as a constituent of the amino acid pool in CSF. For proline and hydroxyproline a special control system has to be suggested because of their smaller biological variance in CSF than in blood. Contrary to the other amino acids proline and hydroxyproline have a smaller biological variation in CSF than in serum.

Adolescent↗
PubMed1984

Primary structure of human class II histocompatibility antigens. Reversed-phase high-performance liquid chromatography for integral membrane proteins.

The amino acid sequence of the human HLA-DR2 class II antigen was determined with the aid of high-performance liquid chromatography. By applying exclusively Hypersil-ODS as the stationary phase in combination with three buffer systems, the amino acid sequences of the extracellular parts of the DR alpha- and DR beta-chains could be established. Moreover, the sensitivity of the procedure allowed the determination of the primary structures of additional class II polypeptides isolated together with the DR2 alpha- and the DR2 beta-chains. Significant insight into the heterogeneity of class II molecules was thereby obtained. In addition, a simple, rapid and selective method of general applicability is described for the isolation of membrane fragments of integral membrane proteins. Using Sep-Pak cartridges with a mobile phase containing 60% formic acid and varying 1-propanol concentrations, the highly hydrophobic peptides can selectively be separated from the hydrophilic fragments.

Amino Acid Sequence↗
PubMed1983

Primary structure of human class II histocompatibility antigens 3rd communication. Amino acid sequence comparison between DR and DC subclass antigens derived from a lymphoblastoid B cell line homozygous at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1).

Class II histocompatibility antigens from a homozygous human lymphoblastoid B cell line (HLA-A3,3; B7,7; Dw2,2; DR2,2; MT1,1; DC1,1; MB1,1) were isolated by an exclusively chemical procedure. After the separation of the alpha and beta chains the amino acid sequences of the extracellular parts of the DR2 alpha and the DR2 beta chains could be determined, in spite of the heterogeneity of both fractions. Peptides isolated in considerably lower yields indicated at least one more alpha chain and 6 further beta chains. By the investigation of these lower-yield enzymatic fragments, in addition to the DR2 alpha and DR2 beta chains, we can now report on the partial amino acid sequences of a DC alpha chain, a second beta chain of DR type and one beta chain of DC type. Furthermore, the isolation of a characteristic glycopeptide suggests the existence of a second beta chain of DC type. The following class II antigens are therefore identified: DR2 alpha/DR2 beta 1, DR2 alpha/DR2 beta 2, DC1 alpha/DC1 beta 1, DC1 alpha/DC1 beta 2, indicating that each subclass can be subdivided into two antigens because each alpha chain type can associate with at least either beta 1 or beta 2. Further investigations must clarify whether the remaining three beta chains are of the DR, DC, or of a third beta chain type. Amino acid sequence comparisons confirm that the human DR antigens are the equivalent of mouse I-E antigens, while human DC antigens are the equivalent of mouse I-A antigens.

Amino Acid Sequence↗
PubMed1983

Hip fractures in the county of Funen, Denmark. Implications of demographic aging and changes in incidence rates.

In patients 40 years and above a total of 3096 hip fractures (783 in males and 2313 in females) occurred in the entire county of Funen, Denmark from 1 July 1973 to 30 June 1979. The incidence of hip fractures increased exponentially with age in both sexes. During the survey the number of hip fractures in females showed a marked increase above what could be explained by demographic aging alone, whereas this tendency was not so pronounced in males. Provided the observed increase in incidence rates prevails, aging of the population in combination with this increase will lead to a threefold increase in the number of hip fractures over a 20-year period. This is substantially more than other Scandinavian authors have reported.

Adult↗
PubMed1982

[Primary structure of class II human histocompatibility antigens. 2nd Communication. Amino acid sequence of the N-terminal 179 residues of the alpha-chain of an HLA-Dw2/DR2 alloantigen (author's transl)].

From a lymphoblastoid homozygous cell-line (HLA-A3,3; B7,7; Dw2,2; DR2,2) the alpha-chain of the HLA-Dw2/DR2 antigen was isolated by an exclusively chemical procedure. The alpha- was separated from the beta-chain by chromatography with hydroxylapatite in Na-dodecyl sulfate. Here we describe the amino acid sequence of the alpha-chain up to Position 179. The molecule is divided into two domains which do not appear homologous to each other but show a significant homology to the beta-chain (21.2%). The similarity is larger in the second (27%) than in the first (15.5%) domain, indicating a different evolutionary relationship for both parts. In contrast to the beta-chain both domains contain an N-glycosidically linked carbohydrate. The methionines are positioned only in the N-terminal, the cysteines exclusively in the C-terminal domain. Only the latter can therefore be stabilized by a disulfide bridge. As with the beta-chain the regions around the cysteines show a remarkable similarity with the constant C-terminal domains of k-, lambda-, alpha-, gamma-, sigma-, epsilon- and mu-chains of immunoglobulins. Although to a considerably lesser extent, the alpha-chain preparation also shows a heterogeneity at the protein level. Since the employed cell-line is homozygous with regard to HLA-D/DR, our results indicate that at least two alpha-chain genes exist in the HLA-D/DR-region. Together with the already published sequence of the beta-chain, the extracellular part of an histocompatibility antigen of the HLA-D type is now known.

Amino Acid Sequence↗