Structure of an antibody combining site by magnetic resonance.

The structure of the combining site of the DNP binding IgA mouse myeloma protein MOPC 315 has been determined by a combination of high resolution nuclear magnetic resonance, electron spin resonance, model building and chemical modifications. This approach yields that general dimensions of the site, its polarity and asymmetry features, the assignment of the DNP-contact residues and their three-dimensional coordinates.     

Differentiation antigens in keratinocytes]

By means of indirect immunofluorescence with human sera it has been demonstrated that cytoplasmic components of the basal cell layer showed antigenic differences as compared to the upper cell layers. Moreover there were differences whether the cells were involved in a mucous, a parakeratinized or an orthokeratinized differentiation.     

Molecular aspects of 2 human urinary glycoproteins with histocompatibility antigen (HLA) serological activity]

Two serologically active urinary glycoproteins (HLA-A 9 and HLA-B 12) were isolated from urine provided by a patient suffering from tubular proteinuria. Their N-terminal sequences were automatically determined. The latter were identical with the sequence of another urinary glycoprotein (protein HC). The relationship between protein HC and the serological activity is discussed.     

Antifertility activity of trimethylphosphate in male rats

Summary The toxic effect of trimethylphosphate on rat testes was investigated after oral dosing with 250 mg/kg for either 5 days/week for 30 days or 6 days/week for 60 days. After these prolonged treatments azoospermia resulted.Acknowledgments. The authors wish to thank Ms M. Michelles, Ms A. Murray and Ms R. Peake for their technical support.     

T4 gene 32 protein model for control of activity at replication fork.

Limited hydrolysis of gene 32 protein by various proteinases results in the production of three stable cleavage products. Two of these products show an affinity for native T4 DNA cellulose that the uncleaved protein does not exhibit. A model for proteolytic cleavage and for the total unwinding of DNA in advance of the replication fork is discussed in terms of this unusual binding affinity.     

125I-Insulin is preferentially internalized in regions of the hepatocytes rich in lysosomal and Golgi structures

Summary ¹²⁵I-Insulin initially localizes to the plasma membrane of isolated rat hepatocytes but is subsequently internalized and preferentially associates with lysosomal structures. In the present study, we show that this preferential association to lysosomes occurs in regions of the cell rich in lysosomal and Golgi structures.This work was performed while Dr Gorden was visiting professor of the Institute of Histology and Embryology, University of Geneva, Geneva, Switzerland.This work was supported by grant No. 3.120.77 from Swiss National Science Foundation. We thank M.M. Sidler-Ansermet, O. Jerotic and N. Maalaoui for their valuable help.