Title : Demonstration of a
glycoprotein derived from the
Ceacam10 gene in mouse seminal vesicle secretions
Abstract :
- C EACAM10 was purified from mouse seminal vesicle secretions by a series of purification steps that included ion exchange chromatography on a DEAE-Sephacel column and ion exchange high-performance liquid chromatography on a sulfopropyl column
- It was shown to be a 36-kDa glycoprotein with an N-linked carbohydrate moiety
- The circular dichromoism spectrum of CEACAM10 in 50 mM phosphate buffer at pH 7.4 appeared as one negative band arising from the beta form at 217 nm
- CEACAM10 was expressed predominantly in seminal vesicles of adult mice
- Both CEACAM10 and its mRNA were demonstrated on the luminal epithelium of the mucosal folds in the seminal vesicle
- The amount of Ceacam10 mRNA in the seminal vesicle was correlated with the stage of animal maturation
- Castration of adult mice resulted in cessation of Ceacam10 expression, while treatment of castrated mice with testosterone propionate in corn oil restored Ceacam10 expression in the seminal vesicle
- During the entire course of pregnancy, Ceacam10 might be silent in the embryo
- A cytochemical study illustrated the presence of the CEACAM10 binding region on the entire surface of mouse sperm
- CEACAM10-sperm binding greatly enhanced sperm motility in vitro
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycoprotein, , glycoprotein, -, -
- 2. glycoprotein, , glycoprotein, an N-linked carbohydrate moiety, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):