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the Role of the Mammalian Sperm Acrosome in Fertilization

Nathlita Karnley, Subir Nagdas, Department of Chemistry and Physics, Fayetteville State University, 1200 Murchison Rd, Fayetteville NC 28301

Mammalian fertilization is accomplished by the interaction between sperm and egg. Previously, we have identified a stable acrosomal matrix assembly from the bovine sperm acrosome termed the outer acrosomal membrane–matrix complex (OMC). This stable matrix assembly exhibits precise binding activity for acrosin and N-acetylglucosaminidase. A highly purified OMC fraction comprises three major (54, 50, and 45 kDa) and several minor (38–19 kDa) polypeptides. The set of minor polypeptides (38–19 kDa) termed ‘‘OMCrpf polypeptides’’ is selectively solubilized by high-pH extraction (pH 10.5), while the three major polypeptides (55, 50, and 45 kDa) remain insoluble. Proteomic identification of the OMC32 polypeptide (32 kDa polypeptide isolated from high-pH soluble fraction of OMC) yielded two peptides that matched the NCBI database sequence of acrosin-binding protein. The present study was undertaken to define the function of OMC32 polypeptide of the acrosome reaction, and to elucidate the potential role of the protein in sperm function.




Additional Abstract Information

Presenter: Nathlita Karnley

Institution: Fayetteville State University

Type: Oral

Subject: Chemistry

Status: Approved


Time and Location

Session: Oral 7
Date/Time: Tue 3:30pm-4:30pm
Session Number: 710
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