Kooperativer Bibliotheksverbund

Berlin Brandenburg


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  • 1
    Language: English
    In: Water Resources Research, 05/1998, Vol.34(5), pp.1241-1249
    Description: Observed data sets containing values above or below the analytical threshold of measuring equipment are referred to as censored. Such data are frequently encountered in quality and quantity monitoring applications of water, soil, and air samples. Most of the previous literature on the statistical analysis of censored data relates to the problems of moment, parameter, and quantile estimation methods. Such estimation methods usually assume an underlying probability distribution. Few goodness-of-fit methods exist for censored data. We introduce L moment diagrams for the evaluation of the goodness of fit of alternative distributional hypotheses for left-censored data. Experiments with artificial censored data sets document the conditions under which L moment diagrams should be useful. Our approach, like Hosking's [1995] approach for right censoring, derived L moment diagrams for left-censored observations from partial probability-weighted moments. Copyright 1998 by the American Geophysical Union.
    Keywords: Hydrogeology ; Environmental Geology ; Data Management ; Environmental Analysis ; Information Management ; Monitoring ; Pollution ; Probability ; Soils ; Statistical Analysis ; Surface Water ; Water Quality;
    ISSN: Water Resources Research
    E-ISSN: 00431397
    E-ISSN: 19447973
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  • 2
    Language: English
    In: Biology of Reproduction, 04/01/1998, Vol.58(4), pp.1057-1064
    Description: P47, a peripherally associated 47-kDa protein of porcine spermatozoa, was identified by affinity chromatography in the fraction of solubilized plasma membrane proteins bound to immobilized porcine zona pellucida glycoproteins. N-terminal and internal amino acid sequences revealed structural similarity between P47 and rat O-acetyl ganglioside synthase, bovine mammary gland protein (MPG)57/53 and mouse milk fat globule protein E8-polypeptides of unknown function secreted by mammary gland epithelial cells in both species. A polyclonal antibody directed against bovine MGP57/53 displayed cross-reactivity with P47. Indirect immunofluorescence analysis located porcine P47 on the acrosomal cap of testicular sperm and on sperm recovered along different sections of the ductus epididymidis, as well as on swim-up and in vitro-capacitated sperm. Porcine P47 was demonstrated on sperm bound to the zona pellucida of a homologous oocyte. Western blot analysis identified P47 (or MGP57/53) homologous proteins in porcine and human milk. Like the sperm-associated protein, porcine milk P47 possesses affinity for isolated, biotinylated sow oocyte zona pellucida glycoproteins. Reverse transcription-polymerase chain reaction was used to isolate P47 homologous cDNAs from porcine testis and mammary gland tissues as well as from bovine, mouse, and human testis. P47 proteins deduced from these cDNA sequences showed 60-100% amino acid sequence identity. These proteins display a mosaic structure organized into two N-terminal, tandemly arranged epidermal growth factor (EGF)-like domains followed by a region with similarity to C1 and C2 domains found in blood clotting factors V and VIII. The second EGF-like domain contains an arginine-glycine-aspartic acid sequence, a motif often found in integrin receptor ligands. P47-like proteins are not expressed solely in testicular and mammary gland tissues. Northern blot analysis showed that P47 mRNA is transcribed in several porcine and bovine tissues. These data indicate a potential role for boar sperm-associated P47 in membrane remodeling and/or as a zona pellucida binding protein.
    Keywords: Structure & Sequence ; Domestic Animals (Pigs) ; O-Acetyl Ganglioside Synthase ; O-Acetyl Ganglioside Synthase ; P47 Protein ; Boars ; Cattle ; Coagulation Factor V ; Coagulation Factor VIII ; Epidermal Growth Factor ; Mammary Gland Protein 57/53 ; Mice ; Milk Fat Globule Protein ; Nucleotide Sequence ; Rats;
    ISSN: 0006-3363
    E-ISSN: 1529-7268
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  • 3
    Language: English
    In: European Journal of Immunology, May 1998, Vol.28(5), pp.1701-1707
    Description: CD97 is an activation‐induced antigen on leukocytes which belongs to a new group of seven‐span transmembrane (7‐TM) molecules, designated EGF‐TM7 family. Family members, including EMR1 and F4/80, are characterized by an extended extracellular region with several N‐terminal epidermal growth factor‐like (EGF) domains. Alternative splicing of CD97 results in isoforms possessing either three (EGF1, 2, 5), four (EGF1, 2, 3, 5) or five EGF domains (EGF1, 2, 3, 4, 5). We recently identified decay accelerating factor (DAF, CD55), a regulatory protein of the complement cascade, as a cellular ligand of the smallest isoform. Employing mutants of CD97(EGF1, 2, 5) in which the EGF domains have been systematically deleted, we here demonstrate the necessity of at least three tandemly linked EGF domains for the interaction with CD55. Consistent with the involvement of different EGF domains, monoclonal antibodies directed against the first EGF domain as well as the removal of Ca , for which binding sites exist in the second and fifth EGF domain, blocked binding to CD55. Compared to CD97(EGF1, 2,5) the larger isoforms CD97(EGF1, 2, 3, 5) and CD97(EGF1, 2, 3, 4, 5) have a significantly lower affinity for CD55. Thus, alternative splicing may regulate the ligand specificity of CD97 and probably other members of the EGF‐TM7 family.
    Keywords: Adhesion ; Egf‐Tm7 Family ; Cd97 ; Cd55 ; Epidermal Growth Factor‐Like Domain
    ISSN: 0014-2980
    E-ISSN: 1521-4141
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