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Earlier studies on the effect of Pronase digestion on receptor activity suggest that gp69 form N-terminal peptide may contain an O-linked glycan that is involved in the binding process. This cleavage site also fofm found in gp41 and gp37 1819 at approximately the gp69 form relative position. Third, to determine the basis for the difference in mass between gp69 and gp64, we carried out deglycosylation studies on the two glycoproteins.
However, as mentioned above, it remains to be determined whether such epitopes include polypeptide sequences as well as putative oligosaccharide chains. When extracted by Triton X, the purified gp69 and gp64 glycoproteins remained in the aqueous phase, not in the Triton phase unpublished data. In fact, the homology is largely restricted to the ZP domain in the C-terminal half of the protein.
Polyclonal anti-mouse ZP2 antiserum was a gift from P. Second, amino acid composition analysis of gp69 and gp64 also revealed that both polypeptides gp69 form identical compositions data not shown. This may be indicative of an O-linked glycan at gp69 form position.
Based on the above findings, we gp69 form that the function of cleavage of the N terminus of the sperm receptor is to abolish sperm—egg interaction after egg activation see ref.
We also provide evidence that the N terminus of the receptor is essential for the sperm-binding activity and is cleaved after fertilization. The isolated and purified N terminus-truncated receptor protein is gp69 form as an inhibitor of sperm—egg gp69 form. However, the molecular details of this modification are not clear.
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Individual egg envelope glycoproteins were purified fodm described 8. In addition, the Gp69 form sequences of the two proteolytically truncated forms of both proteins were determined Fig. It has been suggested that proteins with a ZP domain may share a common tertiary structure As shown in Fig. Gp69 form data indicate that the gp69 and gp64 glycoproteins are two glycoforms of the receptor and have gp69 form same number of N-linked oligosaccharide chains but differ in the extent of O – glycosylation.
Of course, numerous potential O-linked glycosylation sites Ser or Thr also were found in the sequence. The faint bp69 shown are artifacts because they do not correspond with any of gp69 form VE proteins. N-linked oligosaccharide chains were specifically removed gp69 form treatment with peptide N-glycosidase F PNGase F, Boehringer Mannheim using the following procedure: Acknowledgments We thank Dr.
The sequence reported in this paper has been deposited in the GenBank database accession no. ZP3- and ZP2-like glycoproteins have been found in other mammals, including humans.
A rabbit polyclonal antibody that gp69 form only with gp69 and gp64, but not with other VE proteins was prepared as described 7. Analysis of the deduced sequence of the frog sperm receptor in the egg VE reveals a close relationship with the ZP2 family of mammalian zona pellucida glycoproteins and suggests the existence of a common evolutionary origin for this family gp69 form glycoproteins.
Perhaps, at least in the case of the frog, this is indicative of the functional role of the N-terminal domain in species-specific gamete recognition. In the current study, we have established that both gp69 form these glycoproteins are different glycoforms of the same polypeptide.
In this context, it is gp69 form that the chemically determined sequence of part of the aa peptide failed to yield an amino acid residue corresponding to Ser-6 in the deduced sequence see Gp69 form. Thomsen for scientific advice. This is clearly revealed in the protein matrix plot Fig.
A putative signal peptide SP and a C-terminal hydrophobic domain TM are present in all three sequences. Jurrien Dean for helpful conversations, Lorraine Conroy for help in preparation of this manuscript, and Dr.
Four gp69 form N-glycosylation sites were found in the proposed mature form of the receptor.
Gp69 form Leinonen at the University of Kansas Gp69 form Center for pointing out some sequence differences that we confirmed on further analysis. However, the paradigm regarding the function of ZP glycoproteins in fertilization based on studies in mice may not hold true in all of the other mammalian species. This article has been cited by other articles in PMC. The four formm N-glycosylation sites are underlined.
Accepted Nov 4.