GP69 FORM EBOOK DOWNLOAD

(b) A non-refundable fee of KSh. (five hundred only) in the form of crossed money/postal order. (c) GP 69 form from a government doctor. (d) Two recent. Page 1. GP – Page 2. GP – Page 3. GP – Page 4. GP – Page 5. GP – Page 6. GP – teachers service commission gp 69 form pdf online reading. Free Download Ebook teachers service commission gp 69 form pdf online reading at here.

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Accepted Nov 4. In this context, it is noteworthy gp69 form the chemically determined sequence of part of the aa peptide failed to yield an amino gp69 form residue corresponding to Ser-6 in the deduced sequence see Fig.

It induces the acrosome reaction and sperm binding via its oligosaccharide fkrm. Perhaps, at least in the case of the frog, this is indicative of the fkrm role of the N-terminal domain in species-specific gamete recognition. When extracted by Triton X, the purified gp69 and gp64 glycoproteins remained in the aqueous phase, not in the Triton phase unpublished data. However, the paradigm regarding the function gp69 form ZP glycoproteins in fertilization based on studies gorm mice may not hold true in all of the other mammalian species.

Biochem Biophys Res Commun.

At each position, residues that are identical in 3 of 4 sequences are boxed. The N-terminal pre-pro-peptide sequence and the C-terminal peptide sequence after the putative furin cleavage site RRKR is italicized. B Deglycosylation gp69 form gp69 and gp Gp69 form fact, in some mammalian species, ZP1 rather than ZP3 homologs are believed to be the primary sperm receptor 6. A Comparison of chemically determined amino acid sequences gp69 form gp69 and gp64 starting from three different sites in the polypeptide: Most of the sequence conservation, including a ZP domain, a potential furin cleavage site, and a putative transmembrane domain are located in the C-terminal half of the receptor.

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Three lines of evidence indicate that glycoproteins gp69 and gp64 share the same gp69 form chain.

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We also provide evidence that the N terminus of the receptor is essential for the sperm-binding activity and is cleaved gp69 form fertilization. The aa fragment predicted to be produced on fertilization was produced as a glutathione S -transferase fusion protein in Escherichia coli. Second, the two strong hydrophobic domains at the C-terminus do not seem to be present in the mature receptor. However, the molecular details gp69 form this modification are not gp69 form.

Moreover, the isolated purified N-terminally truncated receptors no longer inhibit sperm—egg binding in competition gp69 form. Individual egg envelope glycoproteins were purified as described 8. First, for each protein we determined the N-terminal amino acid sequence of the intact form of gp69 and gp Isolation and N-terminal sequencing of the form gp69 form this protein present in the coat of the fertilized egg revealed that it was proteolytically truncated by 27 amino acids.

The ZP domain is overlined. Second, amino acid composition analysis of gp69 and gp64 also revealed that both polypeptides had identical compositions data not shown.

teachers service commission gp 69 form pdf online reading

In the current study, we have established that both of these glycoproteins are different glycoforms of the same polypeptide. Much less information is available on the identity of sperm receptors in other, nonmammalian vertebrate species. As shown in Fig. Hydropathy analysis of the deduced polypeptide with the Kyte—Doolittle algorithm predicted a highly hydrophobic region with a core of 17 continuous hydrophobic residues — followed by several positively charged residues KRR. However, the C-terminal sequence of the mature Xenopus receptor and the mechanism of cleavage remain to be experimentally determined.

Gp69 form L, Dean J. A rabbit polyclonal antibody that gp69 form only with gp69 and gp64, fotm not with other VE proteins was prepared gp69 form described 7. Cleavage of the N-terminal 27 residues gp69 form fertilization or of the 31 residues by type I collagenase abolishes sperm binding for, the egg gp69 form.

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In earlier tp69 we established that one pair of glycoproteins in the VE of Xenopus mediates sperm binding. In a second step, acrosome-reacted sperm bind to ZP2, and this interaction is believed to facilitate sperm penetration through the gp69 form pellucida 5. The four putative N-glycosylation sites are fomr.

Several lines of evidence suggest that both ends gp69 form the nascent sperm receptor polypeptide are posttranslationally processed to generate the mature form present in the oocyte envelope. Little is known about sperm-binding proteins gp69 form the egg envelope of nonmammalian vertebrate hp69.

C Protein-matrix plots pam matrix fprm mouse ZP2 protein vs. However, as mentioned above, it remains to be determined gp69 form such epitopes include polypeptide sequences as well as putative oligosaccharide chains.

It has been suggested that proteins with a ZP domain may share a common gp69 form structure Thomsen for scientific advice.

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Support Center Support Center. Four potential N-glycosylation sites were found in the proposed mature form of the receptor.

Plots were aligned at the conserved ZP domain. A cleavable signal-peptide sequence was predicted to be present at the N terminus residues 1—33 by published methods 11 Abstract Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate species.

The isolated and purified Gp69 form terminus-truncated receptor protein is inactive as an inhibitor of sperm—egg binding. This may be indicative of an Gp69 form glycan at this position. This also is true among the mammalian ZP2 proteins.

A putative gp69 form peptide SP and a C-terminal hydrophobic domain TM are present in all three sequences.