An N-terminal partial sequence of the 13 kDa Pycnopodia helianthoides sperm chemoattractant 'startrak' possesses sperm-attracting activity.
作者： Richard Vogt , Richard L. Miller
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摘要: Freshwater extracts of starfish ovaries were used to purify the sperm-attracting peptide 'startrak' from Pycnopodia helianthoides using hydrophobic interaction chromatography and DEAE-high-pressure liquid chromatography. Partially purified attractant had a molecular mass 13 kDa, estimated gel filtration polyacrylamide electrophoresis results. The was subjected amino acid analysis direct sequencing, found consist largely single composed an 127 residues based on 13kDa. An N-terminal sequence acids positions 3 34 obtained synthesized as: NH2-Ala-Glu-Leu-Gly-Leu-Cys-Ile-Ala-Arg-Val-Arg-Gln-Gln-Asn-Gln-Gly-Gln- Asp-Asp-Val-Ser-Ile-Tyr-Gln-Ala-Ile-Met-Ser-Gln-Cys-Gln-Ser-COOH. synthetic possessed activity 130 times greater than partially startrak showed pattern species-specificity sperm chemotaxis similar that startrak. Antibody prepared against removed crude preparations partial not homologous with any known echinoid motility-activating peptides.
biologists.org参考文章(48)
H C Lee, D L Garbers, Modulation of the voltage-sensitive Na+/H+ exchange in sea urchin spermatozoa through membrane potential changes induced by the egg peptide speract. Journal of Biological Chemistry. ,vol. 261, pp. 16026- 16032 ,(1986) , 10.1016/S0021-9258(18)66670-0
D L Garbers, H D Watkins, J R Hansbrough, A Smith, K S Misono, The amino acid sequence and chemical synthesis of speract and of speract analogues. Journal of Biological Chemistry. ,vol. 257, pp. 2734- 2737 ,(1982) , 10.1016/S0021-9258(19)81020-7
M. Yamaguchi, N. Suzuki, K.-I. Yoshino, M. Kurita, Speract binds exclusively to sperm tails and causes an electrophoretic mobility shift in a major sperm tail protein of sea urchins Zoological Science. ,vol. 4, pp. 641- 648 ,(1987)
S L Sutrina, P Reddy, M H Saier, J Reizer, The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease. Journal of Biological Chemistry. ,vol. 265, pp. 18581- 18589 ,(1990) , 10.1016/S0021-9258(17)44791-0
D S Thorpe, D L Garbers, The membrane form of guanylate cyclase. Homology with a subunit of the cytoplasmic form of the enzyme. Journal of Biological Chemistry. ,vol. 264, pp. 6545- 6549 ,(1989) , 10.1016/S0021-9258(18)83382-8
L J Dangott, D L Garbers, Identification and partial characterization of the receptor for speract. Journal of Biological Chemistry. ,vol. 259, pp. 13712- 13716 ,(1984) , 10.1016/S0021-9258(18)89803-9
Tatsuo Harumi, Masaaki Yamaguchi, Norio Suzuki, Receptors for sperm-activating peptides, SAP-I and SAP-IIB, on spermatozoa of sea urchins, Hemicentrotus pulcherrimus and Glyptocidaris crenularis Development Growth & Differentiation. ,vol. 33, pp. 67- 73 ,(1991) , 10.1111/J.1440-169X.1991.00067.X
R W Schackmann, P B Chock, Alteration of intracellular [Ca2+] in sea urchin sperm by the egg peptide speract. Evidence that increased intracellular Ca2+ is coupled to Na+ entry and increased intracellular pH. Journal of Biological Chemistry. ,vol. 261, pp. 8719- 8728 ,(1986) , 10.1016/S0021-9258(19)84440-X
N Suzuki, H Shimomura, E W Radany, C S Ramarao, G E Ward, J K Bentley, D L Garbers, A peptide associated with eggs causes a mobility shift in a major plasma membrane protein of spermatozoa. Journal of Biological Chemistry. ,vol. 259, pp. 14874- 14879 ,(1984) , 10.1016/S0021-9258(17)42685-8
G. E. Ward, V. D. Vacquier, Dephosphorylation of a major sperm membrane protein is induced by egg jelly during sea urchin fertilization. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 80, pp. 5578- 5582 ,(1983) , 10.1073/PNAS.80.18.5578