Heterogeneity of cationic amino acid transport systems in mouse mammary gland and their regulation by lactogenic hormones

The mechanism of cationic amino acid transport in lactating mouse mammary gland was investigated. Two Na+-independent systems of arginine transport were discriminated on the basis of their sensitivity to leucine. The leucine-sensitive uptake of arginine (Km 0·4 mM) was through a broad specificity system that interacted with both cationic and neutral amino acids, and was inhibited by preloading mammary tissue with neutral amino acids. The leucine-insensitive uptake was identified as the y+ system (Km 0·76 mM). Preloading mammary tissue with cationic amino acids increased the uptake of arginine by the y+ system. Decreasing the pH of the external medium to 6·0 suppressed the y+ system-mediated uptake by ∼25%, whereas the broad specificity system remained unaffected. Lactogenic hormones upregulated the y+ system-mediated uptake of arginine in pregnant mouse mammary tissue cultured in vitro, although the broad specificity system remained unaffected. The y+ system-mediated uptake increased 2-fold with insulin alone and 4-fold with the combination of insulin, cortisol and prolactin.

Structures and mechanisms of DNA restriction and modification enzymes

DNA restriction and modification enzymes are responsible for the hostspecific barriers to interstrain and interspecies transfer of genetic information that have been observed in a variety of bacterial cell types. Although the phenomenon of host specificity was initially observed in the early 1950s (Luria & Human, 1952; Bertani & Weigle, 1953), it was nearly a decade later that Arber and his colleagues accurately predicted the molecular basis of the phenomenon. Their experiments with bacteriophage λ demonstrated that a given host-specificity system imparts a specific modification to the viral DNA, and further, that restriction of DNA lacking the appropriate modification is s consquence of nucleolytic hydrolysis upon entry into the host cell (Arber & Dussoix, 1962; Dussoix & Arber, 1962; Arber, Hattman & Dussoix, 1963).

A NEW MATING COMPATIBILITY LOCUS IN PHYSARUM POLYCEPHALUM

ABSTRACT The rate and extent of plasmodium formation were studied in mating tests involving pairs of largely isogenic amoeba1 strains compatible for matingtype (mt) alleles. A systematic variability was observed: plasmodia formed either rapidly and extensively or slowly and inefficiently. Plasmodium formation was found to be 103- to 104-fold more extensive in "rapid" crosses than in "slow" crosses. A genetic analysis revealed that the variability reflects the influence of a multiallelic compatibility locus that determines mating efficiency. This compatibility locus (designated matB), together with the original mating type locus mt (in this work designated matA), constitute a tetrapolar mating specificity system in Physarum polycephalum.