Isolation, characterisation and cDNA sequencing of a new form of parvalbumin from carp semen
Mariola A. Dietrich A C , Błażej Westfalewicz A , Patrycja Jurecka B , Ilgiz Irnazarow B and Andrzej Ciereszko A
+ Author Affiliations
- Author Affiliations
A Department of Gamete and Embryo Biology, Semen Biology Group, Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, 10-747 Olsztyn, Poland.
B Institute of Ichthyobiology and Aquaculture of Polish Academy of Sciences, Gołysz, 43-520 Chybie, Poland.
C Corresponding author. Email: m.dietrich@pan.olsztyn.pl
Reproduction, Fertility and Development 26(8) 1117-1128 https://doi.org/10.1071/RD13181
Submitted: 11 July 2013 Accepted: 9 August 2013 Published: 25 September 2013
Abstract
Parvalbumins (Pv) are calcium-binding proteins present mainly in the muscle and nervous system where they act as a Ca2+ buffer. Our previous work demonstrated the presence of Pv-I in carp semen and indicated the presence of a second Pv (Pv-II). The purpose of the present work was to identify, purify and determine the full-length cDNA sequence of Pv-II from carp testis. Pv-II from seminal plasma was purified by ion-exchange chromatography (IEC) and preparative electrophoresis, while the Pv-II from spermatozoa was purified by IEC, gel filtration and preparative electrophoresis. The purified Pv-II was submitted to an analysis of molecular mass, isoelectric point (pI), amino-acid sequence and oligomerisation ability. The amino-acid sequence was used to construct primers and obtain the full-length cDNA sequence of seminal-specific Pv-II from carp testis. Analysis of the cDNA sequence indicated that carp-testis Pv-II was distinct from carp-muscle parvalbumins. Pv-II was distinct from Pv-I regarding sequence, molecular mass and pI. Both parvalbumins had the ability to form oligomers or to bind to other proteins. Carp seminal plasma had a protective effect against parvalbumin oligomerisation. Pv-II underwent post-translational modification such as n-acetylation and cysteinylation. The present study is the first to report the full-length cDNA sequence of parvalbumin from carp testis.
Additional keywords: oligomerisation, seminal plasma, spermatozoa.
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