Two‐dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

Marzocchi, Barbara; Magi, Barbara; Bini, Luca; Cellesi, C; Rossolini, A; Massidda, Orietta; Pallini, Vitaliano

doi:10.1002/elps.11501601140

Cited by 7 publications

References 10 publications

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Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

Magi¹,

Marzocchi²,

Bini³

et al. 1995

Electrophoresis

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Two-dimensional electrophoretograms of serum proteins from ampicillin-treated patients were analyzed-by immunoblotting with an antiserum specific for penicilloyl groups. As expected, human serum albumin (HSA) was the main ampicilloylated serum component. Transferrin main form II was found to be the second most important component as regards immunoblotting intensity. Immunoreactive spots were present on the acidic side of the transferrin isoelectric series, suggesting a modification mechanism similar to that observed in HSA, i.e., acylation of basic amino acid residues. Several additional ampicilloylated spots were detected but could not be assigned. Their electrophoretic parameters were determined using internal standards. This is the first description of serum proteins other than HSA being modified by ampicillin in the course of routine therapeutic treatment.

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Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

Magi¹,

Marzocchi²,

Bini³

et al. 1995

Electrophoresis

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Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression

et al. 1995

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The Us11 protein is a true late gene product of herpes simplex virus type 1 (HSV-1), whose exact function is unknown but which exhibits RNA-binding properties and which is phosphorylated on serine residues. In order to determine whether the Us11 protein is phosphorylated by cellular kinase(s) or by virally encoded kinase(s), the Us11 gene has been cloned and transiently expressed in HeLa cells. In addition, HeLa-derived cell lines have been selected for their ability to express Us11 protein constitutively. 32P-Labeling and analysis by two-dimensional electrophoresis of transiently and constitutively expressed Us11 protein demonstrated that, indeed, multiple phosphorylation of the protein occurs in absence of HSV-1 genome expression, indicating that the protein behaves as a natural substrate for cellular kinase(s). In addition, a sequence heterogeneity of the Us11 protein, due to a difference in the number of SPREPR repeats, has been characterized between different strains of HSV-1.

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Protein Blotting and Immunoblotting

Bini

Liberatori

Magi

et al. 2000

Proteome Research: Two-Dimensional Gel Electrophoresis and Identification Methods

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Two‐dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

Abstract: A two-dimensional gel electrophoresis and immunoblotting procedure has been developed to assess the level of modification by penicillins in human serum albumin. The procedure can be used in in vitro experiments and in clinical studies with sera from patients treated with penicillins.

Cited by 7 publications

References 10 publications

Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression

Protein Blotting and Immunoblotting

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