Complementary Deoxyribonucleic Acid Cloning and Characterization of mSP-10: The Mouse Homologue of Human Acrosomal Protein Sp-101 (original) (raw)

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3Centerfor Recombinant Gamete Contraceptive Vaccinogens, Department of Cell Biology University of Virginia, Charlottesville, Virginia

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3Centerfor Recombinant Gamete Contraceptive Vaccinogens, Department of Cell Biology University of Virginia, Charlottesville, Virginia

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4Department of Molecular Biology, Princeton University, Princeton, NewJersey

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4Department of Molecular Biology, Princeton University, Princeton, NewJersey

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4Department of Molecular Biology, Princeton University, Princeton, NewJersey

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3Centerfor Recombinant Gamete Contraceptive Vaccinogens, Department of Cell Biology University of Virginia, Charlottesville, Virginia

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3Centerfor Recombinant Gamete Contraceptive Vaccinogens, Department of Cell Biology University of Virginia, Charlottesville, Virginia

2Dr. John C. Herr, Department of Cell Biology, P.O. Box 439, School of Medicine, Charlottesville, VA 22908. FAX: (804) 982–3912

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Published:

01 October 1995

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P. Prabhakara Reddi, Soren Naaby-Hansen, Irena Aguolnik, Jen-Yue Tsai, Lee M. Silver, Charles J. Flickinger, John C. Herr, Complementary Deoxyribonucleic Acid Cloning and Characterization of mSP-10: The Mouse Homologue of Human Acrosomal Protein Sp-10, Biology of Reproduction, Volume 53, Issue 4, 1 October 1995, Pages 873–881, https://doi.org/10.1095/biolreprod53.4.873
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Abstract

Complementary DNA encoding the putative mouse homologue for human acrosomal protein SP-10, a candidate contraceptive vaccinogen, was cloned and sequenced. The entire open reading frame (amino acids 18 to 261) of the mouse SP-10 (mSP-10), with the exception of the signal peptide (amino acids 1 to 17), was placed under the influence of inducible T7 RNA polymerase/promoter system to overproduce recombinant protein (re-mSP-10) in Escherichia coli. A six-histidine tag, which was coexpressed at the carboxyl terminus of re-mSP-10, provided the means for purification of re-mSP-10 by immobilized metal chelation affinity chromatography technique. The level of purity of re-mSP-10 thus obtained was determined by 2-dimensional gel electrophoresis to be 98%. Immunoblotting with monoclonal and polyclonal antibodies previously generated against human or baboon SP-10 showed that mSP-10 shared significant antigenic similarity with its primate counterparts. The position of mSP-10 in the mouse genome was next mapped through segregation analysis of an interspecific backcross panel of 96 animals. Acrv1 (assigned gene symbol for mSP-10) was localized in the proximal portion of mouse chromosome 9 in a region that exhibits synteny with human 11q23, the region to which ACRV1 (gene symbol for human SP-10) was previously mapped. These characterizations by combined immunological and gene mapping techniques established the cloned mSP-10 to be the mouse homologue of SP-10.

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copyright © 1995 by The Society for the Study of Reproduction

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