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M R Kula - One of the best experts on this subject based on the ideXlab platform.

  • formation of peptide bonds by Carboxypeptidase C from orange leaves
    1991
    Co-Authors: D Steinke, Schwarz Alexander, Christian Wandrey, M R Kula
    Abstract:

    Carboxypeptidase C partially purified from orange leaves was studied as a Catalyst for enzymatiC peptide synthesis. Various N-proteCted ester- and nuCleophile Compounds were evaluated in order to determine the substrate speCifiCity. For further CharaCterization of the synthetiC reaCtion, optimum pH and the influenCe of the N-terminal proteCting group were studied. KinetiC investigations revealed Considerable differenCes in Km and Vmax for the nuCleophile when the N-terminal proteCting group of the substrate was varied.

D Steinke - One of the best experts on this subject based on the ideXlab platform.

  • formation of peptide bonds by Carboxypeptidase C from orange leaves
    1991
    Co-Authors: D Steinke, Schwarz Alexander, Christian Wandrey, M R Kula
    Abstract:

    Carboxypeptidase C partially purified from orange leaves was studied as a Catalyst for enzymatiC peptide synthesis. Various N-proteCted ester- and nuCleophile Compounds were evaluated in order to determine the substrate speCifiCity. For further CharaCterization of the synthetiC reaCtion, optimum pH and the influenCe of the N-terminal proteCting group were studied. KinetiC investigations revealed Considerable differenCes in Km and Vmax for the nuCleophile when the N-terminal proteCting group of the substrate was varied.

Schwarz Alexander - One of the best experts on this subject based on the ideXlab platform.

  • formation of peptide bonds by Carboxypeptidase C from orange leaves
    1991
    Co-Authors: D Steinke, Schwarz Alexander, Christian Wandrey, M R Kula
    Abstract:

    Carboxypeptidase C partially purified from orange leaves was studied as a Catalyst for enzymatiC peptide synthesis. Various N-proteCted ester- and nuCleophile Compounds were evaluated in order to determine the substrate speCifiCity. For further CharaCterization of the synthetiC reaCtion, optimum pH and the influenCe of the N-terminal proteCting group were studied. KinetiC investigations revealed Considerable differenCes in Km and Vmax for the nuCleophile when the N-terminal proteCting group of the substrate was varied.

Christian Wandrey - One of the best experts on this subject based on the ideXlab platform.

  • formation of peptide bonds by Carboxypeptidase C from orange leaves
    1991
    Co-Authors: D Steinke, Schwarz Alexander, Christian Wandrey, M R Kula
    Abstract:

    Carboxypeptidase C partially purified from orange leaves was studied as a Catalyst for enzymatiC peptide synthesis. Various N-proteCted ester- and nuCleophile Compounds were evaluated in order to determine the substrate speCifiCity. For further CharaCterization of the synthetiC reaCtion, optimum pH and the influenCe of the N-terminal proteCting group were studied. KinetiC investigations revealed Considerable differenCes in Km and Vmax for the nuCleophile when the N-terminal proteCting group of the substrate was varied.

Clelia Ferreira - One of the best experts on this subject based on the ideXlab platform.

  • identifiCation of midgut miCrovillar proteins from tenebrio molitor and spodoptera frugiperda by Cdna library sCreenings with antibodies
    2007
    Co-Authors: Alexandre Ferreira, Plinio T Cristofoletti, D M Lorenzini, L O Guerra, Paulo Bandiera Paiva, Marcelo R S Briones, Walter R Terra, Clelia Ferreira
    Abstract:

    The objeCtive of this study was to identify midgut miCrovillar proteins in inseCts appearing earlier (Coleoptera) and later (Lepidoptera) in evolution. For this, Cytoskeleton-free midgut miCrovillar membrane from Spodoptera frugiperda (Lepidoptera) and Tenebrio molitor (Coleoptera) were used to raise antibodies. These were used for sCreening midgut CDNA expression libraries. Positive Clones were sequenCed, assembled and searChed for similarities with gene/protein databases. The prediCted midgut miCrovillar proteins from T. molitor were: CoCkroaCh allergens (unknown funCtion), peritrophins (peritrophiC membrane proteins), digestive enzymes (aminopeptidase, α-mannosidase) and unknown proteins. PrediCted S. frugiperda midgut proteins may be grouped into six Classes: (a) proteins involved in proteCtion of midgut (thioredoxin peroxidase, aldehyde dehydrogenase, serpin and juvenile hormone epoxide hydrolase); (b) digestive enzymes (astaCin, transporter-like amylase, aminopeptidase, and Carboxypeptidase); (C) peritrophins; (d) proteins assoCiated with miCroapoCrine seCretion (gelsolin, annexin); (e) membrane-tightly bound-Cytoskeleton proteins (fimbrin, Calmodulin) and (f) unidentified proteins. The novel approaCh is Compared with others and miCrovillar funCtion is disCussed in the light of the prediCted proteins.