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Biomedical subjects

H Jensen

Publications and source records attributed to H Jensen.

At least 199 records · Page 11Linked to original sources
PubMed1975

Immunological characterization of human glomerular basement membrane antigens.

Normal human glomerular basement membrane (H-GBM) was solubilized by collagenase and subjected to crossed immunoelectrophoresis with rabbit antibodies against H-GBM. Seven precipitates appeared with the mobility of alpha, beta, and gamma globulins. Only two of these precipitates might be specific for GBM, since the other precipitates disappeared after absorption of the antiserum with liver and placenta. In normal human urine one precipitate, cross-reacting with one of the H-GBM precipitates, was found; this precipitate could also be demonstrated in human placenta and liver.

Antibodies↗
PubMed1975

Bone mineral content in the forearm measured by photon absorptiometry. Principles and reliability.

A method for estimating total bone calcium is reported. The method is based on two-dimensional scanning photon absorptiometry on the distal part of the forearm. The following factors are investigated: precision of measurements on standards and human subjects; linearity; the effect of varying bone orientation; amount of fat and soft tissue; and the relation between weight and content of calcium and phosphate. The results show that the method is eminently suitable for rapid, easy, and atraumatic measurement of local bone calcium in vivo.

Adult↗
PubMed1975

Histochemical demonstration of an LNA-splitting enzyme in the cerebellum of the rat. A aminopeptidase-like reaction localized selectively in the granular layer with acid pH optimum.

Histochemical investigations of leucine aminopeptidase using LNA (L-leucyl-beta-napthylamide) as a substrate reveals a marked enzyme activity selectively localized to the granular layer with inconspicuous reaction in the stratum moleculare and the Purkinje cells in the rat cerebellum. The LNA-splitting enzyme differs from the well-known leucine aminopeptidase (LAP) by its optimum at pH 5.5. The necessary long incubation period used in the present study, and its focal precipitation of the enzyme reaction product in the same place, like acid phosphatases, in the granular layer, suggest a lysosomal localization. The functional role of the LNA-splitting enzyme has been discussed; it is considered that it is involved not only in the protein transformation for synaptic function, but may perhaps also play an important pathogenic role in necrosis, atrophy or even autolysis.

Animals↗
PubMed1974

Macrophage-lymphocyte clusters in the immune response to soluble protein antigen in vitro. II. Ultrastructure of clusters formed during the early response.

Macrophage-lymphocyte clusters are formed when lymph node cells and autologous peritoneal exudate cells from guinea pigs immunized with tubercle bacilli are cultured in the presence of purified protein derivative of tuberculin (PPD) for 20 h. We have studied the ultrastructure of these clusters employing transmission and scanning electron microscopy. The most simple macrophage-lymphocyte cluster consisted of one macrophage, one large central lymphocyte with a blastoid appearance attached to the macrophage with a broad area of contact, and from a few to more than 20 small peripheral lymphocytes attached to the central lymphocyte by their uropods. Some clusters were of more complex type, containing two or three macrophages or one macrophage with more than one central lymphocyte attached to the surface, but even in these clusters each peripheral lymphocyte was attached only to one central lymphocyte. By morphological criteria the peripheral lymphocytes were T lymphocytes.

Animals↗