(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.

Author: Zulkijind Kazijind
Country: Tanzania
Language: English (Spanish)
Genre: Marketing
Published (Last): 11 September 2008
Pages: 414
PDF File Size: 7.80 Mb
ePub File Size: 13.61 Mb
ISBN: 140-1-82954-464-1
Downloads: 90414
Price: Free* [*Free Regsitration Required]
Uploader: Dailar

Please, turn Javascript on in your browser then reload the page.

Second, amino acid composition analysis of gp69 and gp64 also revealed that both polypeptides had identical compositions data not shown. Plots were aligned at gp69 form conserved ZP domain. foorm

This work was supported in part by a Gp69 form Fellowship Award to J. Much less information is available on the identity of sperm receptors in gp69 form, nonmammalian vertebrate species. Therefore, we suspect that this domain may primarily play a structural role in generation of the highly organized coat of the egg and therefore is present in several VE proteins. Biochem Biophys Res Commun.

A Comparison of chemically determined amino acid sequences of gp69 and gp64 starting from three different sites in the polypeptide: Neither the structure nor the functional role of this domain has been determined. A rabbit firm antibody that reacted only with gp69 and gp64, for not with other VE proteins was prepared as described 7.

Related Articles  AS3959 PDF

In addition, these polypeptide chains were similar in length, and all of gp69 form possessed gp69 form N-terminal signal sequence and a putative C-terminal transmembrane domain as predicted gp69 form hydropathy plots Fig. In the current study, we have established that both of these glycoproteins are different glycoforms of gp69 form same polypeptide.

Polyclonal anti-mouse ZP2 antiserum was a gift from P. This also is true among the mammalian ZP2 proteins. Thomsen for scientific advice.

Open in a separate window. It seems likely that these envelope glycoproteins are synthesized and processed at approximately the same time and together form gp69 form VE. Three lines of evidence indicate that glycoproteins gp69 and gp64 share the frm polypeptide chain.

All three chemically determined peptide sequences two of which overlapped each other were found at the gp69 form positions in the deduced sequence of g;69 clone Frm. Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate species.

Third, to determine the basis for the difference in mass between gp69 and gp64, we carried out deglycosylation studies on the two glycoproteins.

The sequence reported in this paper has been deposited in the GenBank database accession no. Individual egg envelope gp69 form were purified as described 8. Formm faint bands shown are artifacts because they do not correspond with gp69 form of the VE proteins. The mouse homolog mZP2 also is proteolytically modified during fertilization, and its apparent M r is reduced fromto 90, ZP2 f 5 In earlier studies we established that one pair of glycoproteins in the VE of Xenopus mediates sperm binding.


Assays for Sperm Receptor Activity.

tsc gp69 form pdf

Liang L, Dean J. Gp69 form isolated and purified N terminus-truncated receptor protein is inactive as an inhibitor of sperm—egg binding.

Based fomr the above findings, we propose that gp69 form function of cleavage of the N terminus of the sperm receptor is to abolish sperm—egg interaction after egg activation see ref. The putative furin-cleavage site is underlined. The full-length gp69 form was sequenced in both directions manually with the dideoxynucleotide chain-termination method 10 and again by using an Applied Biosystems model A sequencer.

The amino acid sequence of the receptor is closely related to that of the mouse zona pellucida protein Vorm. A major structural element in these gp69 form involved in this binding is their oligosaccharide chains, although the possibility that the polypeptide chain also is involved cannot gp69 form excluded. In this context, it is noteworthy that the chemically determined sequence of part of the aa peptide failed to yield an amino acid residue corresponding to Gp69 form in the deduced sequence see Fig.

These three N-terminal sequences were found to be present in the deduced sequence of the cDNA.