Merilisa T Bozzini

age ~60

from San Francisco, CA

Also known as:
  • Meri Lisa Bozzini
  • Meri L Bozzini
  • Lisa Handy

Merilisa Bozzini Phones & Addresses

  • San Francisco, CA
  • South Lake Tahoe, CA
  • San Mateo, CA
  • Emerald Hills, CA
  • Burlingame, CA
  • El Dorado, CA

Us Patents

  • Acetic Anhydride Activation For C-Terminal Protein Sequencing

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  • US Patent:
    54688434, Nov 21, 1995
  • Filed:
    Sep 8, 1994
  • Appl. No.:
    8/302154
  • Inventors:
    Victoria L. Boyd - San Carlos CA
    MeriLisa Bozzini - Burlingame CA
    G. Marc Loudon - West Lafayette IN
  • Assignee:
    Perkin-Elmer - Norwalk CT
  • International Classification:
    C07K 110
    G01N 3368
  • US Classification:
    530345
  • Abstract:
    A method is provided for C-terminal sequencing of a protein or peptide. An important feature of the method is the formation of an oxazolone moiety at the C-terminus of a protein or peptide by treatment with acetic anhydride under basic conditions followed by conversion of the oxazolone to a thiohydantoin moiety by treatment with thiocyanate under acidic conditions. Yields of thiohydantoin are further enhanced by delivering thiocyanate as the conjugate acid of a sterically hindered alkylammnonium cation.
  • Method Of Forming N-Protected Amino Acid Thiohydantoins

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  • US Patent:
    53044975, Apr 19, 1994
  • Filed:
    Jul 15, 1992
  • Appl. No.:
    7/914280
  • Inventors:
    Victoria L. Boyd - San Carlos CA
    MeriLisa Bozzini - San Mateo CA
    Piotr J. Guga - San Mateo CA
    Gerald Zon - San Carlos CA
  • Assignee:
    Applied Biosystems, Inc. - Foster City CA
  • International Classification:
    C07K 102
  • US Classification:
    436 89
  • Abstract:
    A method of forming a thiohydantoin from an N-protected amino acid. The method employs a uronium or phosphonium compound to activate the terminal carboxyl group of the amino acid and a thiocyanate reagent to cyclize the activated amino acid to the thio-hydantoin. The thiohydantoin can be cleaved from its N-protecting group, for use in C-terminal peptide sequencing. Particularly preferred uronium compounds include salts of 2-chlorouronium. Preferred thiocyanate reagents include trimethylsilyl isothiocyanate and crown ether adducts of metallothiocyanates, such as the 18-crown-6 adduct of KSCN.
  • Thiohydantoin Formation And Selective Modification Of The Carboxy Terminus Of An Aspartic Acid- And/Or Glutamic Acid-Containing Protein

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  • US Patent:
    56656033, Sep 9, 1997
  • Filed:
    Jul 8, 1994
  • Appl. No.:
    8/272496
  • Inventors:
    Victoria L. Boyd - San Carlos CA
    MeriLisa Bozzini - Burlingame CA
    Robert J. DeFranco - San Carlos CA
  • Assignee:
    The Perkin-Elmer Corporation - Foster City CA
  • International Classification:
    A61K 3802
  • US Classification:
    436 90
  • Abstract:
    A method of forming a thiohydantoin from an N-protected amino acid is described. The method employs a phosphate compound selected from the group consisting of (R. sub. 1 O)(R. sub. 2 O)P(. dbd. O)X and (R. sub. 1 O)(R. sub. 2 O)P(. dbd. O)--O--P(. dbd. O)(OR. sub. 3)(OR. sub. 4) to form acylphosphate moieties from the carboxyl groups of internal aspartic acid and glutamic acid residues and an acylphosphate moiety at a C-terminal carboxyl. The later acylphosphate, unlike the internal acylphosphates, spontaneously cyclizes to an oxazolone, which is less reactive with nucleophilic reagents. R. sub. 1 and R. sub. 2 are each alkyl, aryl, or alkaryl groups which are the same or different and which may be covalently linked to each other; R. sub. 3 and R. sub. 4 are each alkyl, aryl, or alkaryl groups which are the same or different and which may be covalently linked to each other; and X is a leaving group, such as chlorine or bromine, which is substantially unreactive towards thiohydantoins. The acylphosphate and oxazolone moieties are then reacted with a thiocyanate reagent under conditions effective to convert the internal acylphosphates to amides and the terminal oxazolone to thiohydantoin, thereby permitting selective C-terminal thiodantionation of aspartic acid- and/or glutamic acid-containing proteins.

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