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Yoshiki Sugita

Researcher at Ibaraki Prefectural University of Health Sciences

Publications -  5
Citations -  296

Yoshiki Sugita is an academic researcher from Ibaraki Prefectural University of Health Sciences. The author has contributed to research in topics: Glutathione peroxidase & Epididymis. The author has an hindex of 5, co-authored 5 publications receiving 287 citations.

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Journal ArticleDOI

A porcine homolog of the major secretory protein of human epididymis, HE1, specifically binds cholesterol.

TL;DR: It was found that the He1 homolog is a major cholesterol-binding protein in the porcine epididymal fluid and the possibility that the HE1 homology is involved in the regulation of the lipid composition of the sperm membranes during the maturation in epidIDymis is discussed.
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Molecular cloning and characterization of the epididymis-specific glutathione peroxidase-like protein secreted in the porcine epididymal fluid.

TL;DR: An immunocytochemical study showed that this protein was found to bind to the acrosomal region of the epididymal sperm and to disappear during the acosome reaction, which strongly suggest that thisprotein is enzymatically quiescent at least in the porcine epididylal fluid.
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Characterization of cytosolic glutathione S-transferase in cultured astrocytes

TL;DR: Data suggest that the same types of GST isozymes are expressed in the astrocytes and liver, and take part mainly in the detoxification of 4HNE, which is found to be similar to each other.
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Stage-specific expression of a mouse homologue of the porcine 135kDa alpha-D-mannosidase (MAN2B2) in type A spermatogonia.

TL;DR: The cDNA encoding a mouse homologue of porcine epididymis-specific 135kDa alpha-D-mannosidase (MAN2B2, D28521) was cloned from the mouse testis cDNA library and expressed can serve as a good marker for the late stages of type A spermatogonia and may have an important role to play in the early step of sperMatogenesis in mice.
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Purification and properties of major α-d-mannosidase in the luminal fluid of porcine epididymis

TL;DR: The results suggest that the lysosomal type α- d -mannosidase is the predominantly active enzyme in the luminal fluid of porcine epididymis and that it participates in the glycoprotein modification on the sperm surface during epididykal transit.