5 research outputs found

    Logistic network profitability analysis: a new computing method

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    Este artigo apresenta um método de cálculo de rentabilidade econômica de unidades operacionais (UOs) de empresas de transporte de carga fracionada que operam através de uma rede logística com múltiplas UOs. O cálculo da rentabilidade econômica de cada uma destas UOs é um problema complexo. Devido ao intercâmbio de cargas entre UOs, as receitas de uma UO estão interligadas com as receitas de outras UOs. Os métodos tradicionais de contabilização enfrentam dificuldades quando empregados para determinar a rentabilidade econômica de UOs de uma rede logística de UOs interdependentes. O método descrito neste artigo elimina estas dificuldades por meio do conceito de margem de contribuição.This paper offers a method for evaluating the profitability of operation sites (OS) of less-than-truckload (LTL) carriers conveying shipments through a network with multiple OS. The evaluation of the profitability of each one of these OS is a complex problem. Due to exchanges of shipments between OS, the revenues of one OS are intertwined with the revenues of other OS. Traditional accounting methods show themselves cumbersome when employed to evaluate the profitability of OS of a logistical network of interdependent OS. The method described in this paper overcomes these difficulties by means of the concept of contribution margin

    Rentabilidade econômica de unidades operacionais de uma rede logística: novo método de cálculo

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    <span style="font-family: TimesNewRoman; font-size: xx-small;"><span style="font-family: TimesNewRoman; font-size: xx-small;"><p align="left">Este artigo apresenta um método de cálculo de rentabilidade econômica de unidades operacionais (UO’s) de empresas de transporte de carga fracionada que operam através de uma rede logística com múltiplas UO’s. O cálculo da rentabilidade econômica de cada uma destas UO’s é um problema complexo. Devido ao intercâmbio de cargas entre UO’s, as receitas de uma UO estão interligadas com as receitas de outras UO’s. Os métodos tradicionais de contabilização enfrentam dificuldades quando empregados para determinar a rentabilidade econômica de UO’s de uma rede logística de UO’s interdependentes. O método descrito neste artigo elimina estas dificuldades por meio do conceito de margem de contribuição.</p></span></span&gt

    PEX12, the Pathogenic Gene of Group III Zellweger Syndrome: cDNA Cloning by Functional Complementation on a CHO Cell Mutant, Patient Analysis, and Characterization of Pex12p

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    Rat PEX12 cDNA was isolated by functional complementation of peroxisome deficiency of a mutant CHO cell line, ZP109 (K. Okumoto, A. Bogaki, K. Tateishi, T. Tsukamoto, T. Osumi, N. Shimozawa, Y. Suzuki, T. Orii, and Y. Fujiki, Exp. Cell Res. 233:11–20, 1997), using a transient transfection assay and an ectopic, readily visible marker, green fluorescent protein. This cDNA encodes a 359-amino-acid membrane protein of peroxisomes with two transmembrane segments and a cysteine-rich zinc finger, the RING motif. A stable transformant of ZP109 with the PEX12 was morphologically and biochemically restored for peroxisome biogenesis. Pex12p was shown by expression of bona fide as well as epitope-tagged Pex12p to expose both N- and C-terminal regions to the cytosol. Fibroblasts derived from patients with the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III) were also complemented for peroxisome biogenesis with PEX12. Two unrelated patients of this group manifesting peroxisome deficiency disorders possessed homozygous, inactivating PEX12 mutations: in one, Arg180Thr by one point mutation, and in the other, deletion of two nucleotides in codons for (291)Asn and (292)Ser, creating an apparently unchanged codon for Asn and a codon 292 for termination. These results indicate that the gene encoding peroxisome assembly factor Pex12p is a pathogenic gene of CG-III peroxisome deficiency. Moreover, truncation and site mutation studies, including patient PEX12 analysis, demonstrated that the cytoplasmically oriented N- and C-terminal parts of Pex12p are essential for biological function
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