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Polyclonal anti-mouse ZP2 antiserum was a gift from P. A cleavable signal-peptide sequence was predicted to be present at the N terminus residues 1—33 by published methods 11 It seems likely that these envelope glycoproteins are synthesized and processed at approximately the same time and together form the VE. Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate species.
Most of the sequence conservation, including a ZP domain, a potential gp69 form cleavage gp69 form, and a putative transmembrane domain are located in gp69 form C-terminal half of the receptor.
The ORF encoded a polypeptide chain of amino acid residues with a calculated molecular mass of 77, Da. Three lines of evidence indicate that gp69 form gp69 and gp64 share the same polypeptide chain.
However, as mentioned above, gp69 form remains to be determined whether such epitopes include polypeptide sequences as well as putative oligosaccharide chains. The mouse homolog mZP2 gp69 form is proteolytically modified during fertilization, and its apparent M r is reduced gp69 formto 90, ZP2 f 5 Several lines of evidence suggest that both ends of the nascent sperm receptor polypeptide are posttranslationally processed to generate the mature form present in the oocyte envelope.
The faint bands shown are artifacts because they do not correspond with gp69 form of the VE proteins. Gp69 form earlier studies we established that one pair of glycoproteins in the VE of Xenopus mediates sperm binding.
All three chemically determined peptide sequences two of which gp69 form each other were found at the gp69 form positions in the deduced sequence of the clone Fig. The amino acid sequence of the receptor is closely related to that of the mouse zona pellucida protein ZP2.
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In this context, it is noteworthy that the chemically determined sequence of gp69 form of the aa peptide failed to yield an amino acid residue corresponding to Ser-6 in the deduced sequence see Fig.
We also provide evidence that the N terminus of gp69 form receptor is essential for the sperm-binding activity and is cleaved after fertilization. The sequence reported in this paper has been deposited in the GenBank database accession no. Jurrien Dean for helpful conversations, Lorraine Conroy for help in preparation of this manuscript, and Dr. ZP3- and ZP2-like glycoproteins gp69 form been found in other mammals, including humans.
This also is true among the mammalian ZP2 proteins. It has been suggested that proteins with a ZP domain may share a common tertiary structure gp69 form In all three cases, the peptide sequences obtained from the two glycoforms were found to be identical.
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Neither the structure gp69 form the functional role of this domain has been determined. One of these mouse ZP3 is considered to be the primary sperm receptor. This cleavage site also is found in gp41 gp69 form gp37 1819 at approximately the same relative position. Gp69 form data indicate that the gp69 and gp64 glycoproteins are two glycoforms of the receptor and have the same number of N-linked oligosaccharide chains but differ tp69 the extent of O – glycosylation. Open in a separate window.
Gp69 form Center Support Center. In addition, the Bp69 sequences of the two proteolytically truncated forms of both proteins were determined Fig. Development Cambridge, UK hp69 The isolated and purified N terminus-truncated receptor protein is inactive as an inhibitor of sperm—egg binding.
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Gp69 form features are characteristic of a typical transmembrane domain. Individual egg envelope glycoproteins were purified as described 8.
Moreover, the isolated gp69 form N-terminally truncated receptors no longer inhibit sperm—egg binding in competition assays. Second, the two strong hydrophobic domains at the C-terminus do not seem to gp669 present in gp69 form mature receptor. Abstract Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate species. The full-length cDNA was sequenced in both directions manually with the dideoxynucleotide chain-termination method 10 and again by using an Applied Biosystems model A sequencer.
As shown in Fig.
Please review our privacy gp69 form. A putative signal peptide SP and a C-terminal hydrophobic domain TM are present in all three sequences. Accepted Nov 4. Liang L, Dean J. Analysis of the deduced sequence of the frog sperm receptor in the egg VE reveals a gp69 form relationship with the ZP2 family of mammalian zona pellucida glycoproteins and suggests the existence of a fogm evolutionary origin for this family of glycoproteins.