Arylsulfatase B synthesis and clearance in inbred mouse strains

Arylsulfatase B activity levels were approximately 2-3-fold higher in adult C57BL/6J liver and kidney compared to corresponding tissues from A/J inbred mice. In vivo incorporation of tritiated leucine into C57BL/6J hepatic arylsulfatase B reached a maximum approximately 15 h after injection. The label was cleared from C57BL/6J arylsulfatase B with an apparent half-life of 36 h. The relative rates of synthesis of C57BL/6J and A/J arylsulfatase B were similar; however, the A/J enzyme was cleared more rapidly from liver tissue. C57BL/6J kidney arylsulfatase B appeared to be synthesized at a 2-3-fold higher rate than the corresponding A/J enzyme. These trends suggest genetic regulation of arylsulfatase B is effected through different means in liver and kidney from adult mice of these two inbred strains.     

Experimental study in rats to reduce carbon monoxide in the blood induced by cigarette smoke, by inhaling oxygen at atmospheric pressure]

When animals are exposed to cigarette smoke, the concentration of carbon monoxide in blood is rapidly increased, so that intensive inhalation tests cannot be carried out. A simple apparatus is described to expose Rats alternatively to cigarette smoke and to oxygen in order to reduce the concentration of carbon monoxide in the blood. This method makes it possible to increase the daily administration of smoke considerably; nevertheless, under such conditions, lung tumors were not observed.     

Murine arylsulfatase C: Evidence for two isozymes

Summary SWR/J mice posses high arylsulfatase C, estrone sulfatase, and dehydroepiandrosterone sulfatase activities in liver, spleen and kidney compared to A/J mice. This internstrain activity variation appears to be determined by at least 1 autosomal gene. Murine arylsulfatase C activity occurs in both hydrophobic and hydrophilic forms which differ with respect to certain biochemical properties and exhibit different subcellular distributions. The hydrophilic isozyme is a major component in kidney and brain extracts and a minor isozyme in liver and spleen extracts. The hydrophobic arylsulfatase C isozyme appears to be identical to steroid sulfatase. The hydrophilic arylsulfatase C isozyme does not possess steroid sulfatase activity; however, hydrophilic and hydrophobic arylsulfatase C share certain properties, suggesting that they may be structurally related. The autosomal gene(s) affects both arylsulfatase isozymes.This research was supported in part by National Institutes of Health grant GM 27707.     

Mammalian arylsulfatases A and B: relative rates of hydrolysis of artificial substrates

Summary Rodent and bovine arylsulfatase B hydrolyze 4-methylumbelliferyl sulfate (4MUS) 10- to 30-fold more efficiently than arylsulfatase A. Therefore, 4MUS grossly underestimates arylsulfatase A activity in the presence of excess arylsulfatase B.     

Leaky +1 and -1 frameshift mutations at the same site in a yeast mitochondrial gene

Two mutations in a mitochondrial structural gene, which cause leaky premature polypeptide chain termination and leaky growth, are +1 and -1 frameshifts in the same run of five T residues. The partial restoration of reading frame is probably due to ribosomal frameshifting at this site, and may be promoted by the unique structure of the yeast mitochondrial t RNAPhe.     

Processing of a minimal antigenic peptide alters its interaction with MHC molecules

Before their recognition by T lymphocytes, protein antigens generally require processing by antigen-presenting cells. In a poorly understood series of events, the protein antigen is internalized, transformed and re-expressed on the surface of the antigen-presenting cell in association with gene products of the major histocompatibility complex (MHC). Small peptides derived from the native protein can be recognized in the absence of antigen processing, suggesting that processing involves proteolytic degradation. These peptides are thought to mimic the naturally produced peptide fragment. We describe here a synthetic peptide antigen of this type which does not require processing but which is nevertheless further processed by splenic antigen-presenting cells. Interestingly, this processing event specifically alters the interaction of the peptide with the class II MHC (Ia) molecule, markedly affecting both its potency as an antigen in vitro and its immunogenicity in vivo (IR gene control).