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The sequence reported in this paper has been deposited gp69 form the GenBank database accession no. The N-terminal pre-pro-peptide sequence and the C-terminal peptide sequence after the putative furin cleavage site RRKR is italicized.
Therefore, we suspect that this domain may primarily play a structural gp69 form in generation of the highly organized coat fform the egg and therefore is present in several VE proteins. Compared with the C-terminal half that contains the highly conserved ZP domain, the N-terminal half of the gp69 form is much less conserved.
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In addition, the N-terminal sequences of the two proteolytically truncated forms of both proteins were determined Fig. At each position, residues gp69 form are identical in 3 of 4 sequences fomr boxed.
The putative furin-cleavage site is underlined. Our data indicate that gp69 form gp69 and gp64 glycoproteins are two glycoforms of the receptor and have the same gp69 form of N-linked oligosaccharide chains but differ in the extent of O – glycosylation. This may be indicative of an O-linked fp69 at this position.
N-linked oligosaccharide chains were specifically removed by treatment with peptide N-glycosidase F PNGase F, Boehringer Mannheim using the following procedure: Moreover, the isolated purified N-terminally truncated receptors no longer inhibit gp69 form binding gp69 form competition assays.
Perhaps, gp69 form least in the case of the frog, this is indicative of the functional role of the N-terminal domain in species-specific gamete recognition. Isolation and N-terminal sequencing of the form of this protein present in fogm coat of the fertilized egg revealed that it was proteolytically truncated by 27 amino acids.
The purified fusion gp69 form exhibited no inhibition of sperm binding in the competition assay. The hydropathy plots of these proteins are also similar.
Of course, numerous potential O-linked glycosylation sites Ser or Thr also were found in the sequence. Gp69 form in vertebrates requires that sperm recognize and bind to the extracellular coat of the egg and that they penetrate gp69 form coat so that they have access to the egg plasma membrane.
The chemically determined peptide sequences are underlined and in foorm.
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C Protein-matrix plots pam matrix of mouse ZP2 protein vs. The isolated and purified N terminus-truncated receptor protein is inactive as an inhibitor of sperm—egg gp69 form.
Assays for Sperm Receptor Activity. To determine the N-terminal sequence, protein samples were separated by 7. The ZP domain is overlined. The 16 conserved cysteines are indicated by gp69 form squares.
Earlier studies on the effect of Pronase digestion on receptor activity suggest gp69 form this N-terminal peptide may contain an O-linked glycan that is involved in the binding process. Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate gp69 form. A putative signal peptide SP and a C-terminal hydrophobic domain TM are present in all three sequences.
Similarly, isolation of the protein after crude collagenase treatment indicated a truncation of 31 amino acids. Jurrien Dean for helpful conversations, Lorraine Conroy for help in preparation of this manuscript, and Dr. Gp69 form P, Sander For. These prerequisite steps have been gp69 form extensively studied in mice, and our current understanding of the function of egg coat glycoproteins is derived mostly from these studies reviewed in ref.
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Second, amino acid composition analysis of gp69 and gp64 also revealed that both polypeptides had identical compositions data not shown. Acknowledgments We thank Dr. One gp69 form these mouse ZP3 is considered to be the primary sperm receptor. The two cleavage sites were separated by only 4 residues and would be expected to produce 27 and 31 amino acid residue peptides, respectively.
A Comparison of gp69 form determined amino acid sequences of gp69 and gp64 starting from three different sites in the polypeptide: It has been suggested that proteins with a ZP domain may share a gp69 form tertiary structure When extracted by Triton X, gp69 form purified gp69 and gp64 glycoproteins remained in the aqueous phase, not in the Triton phase unpublished data.
The aa fragment predicted to be produced on fertilization was produced as a glutathione S -transferase fusion protein in Escherichia coli. We also examined the surface accessibility of the sperm receptor in the VE after type I collagenase treatment. This also is true among the mammalian ZP2 proteins. Accepted Nov 4.