Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma

Bovine seminal plasma was submitted to chromatography on Con A-Sepharose. The "noninteracting", "weakly-interacting" and "strongly-interacting" fractions were analyzed through UV-MALDI-TOF MS together with a subfraction of the "non-interacting" material, using...

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Autores principales: Cerezo, Alberto Saúl, Giudicessi, Silvana Laura, Erra Balsells, Rosa, Marquínez, Ana Claudia
Publicado: 2007
Materias:
Bovine seminal plasma
Glyco)proteins
Nor-harmane
Sinapinic acid
UV-MALDITOF MS
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1880554X_v45_n4_p267_Cerezo
http://hdl.handle.net/20.500.12110/paper_1880554X_v45_n4_p267_Cerezo
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_1880554X_v45_n4_p267_Cerezo
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spelling paper:paper_1880554X_v45_n4_p267_Cerezo2023-06-08T16:30:19Z Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma Cerezo, Alberto Saúl Giudicessi, Silvana Laura Erra Balsells, Rosa Marquínez, Ana Claudia Bovine seminal plasma Glyco)proteins Nor-harmane Sinapinic acid UV-MALDITOF MS Bovine seminal plasma was submitted to chromatography on Con A-Sepharose. The "noninteracting", "weakly-interacting" and "strongly-interacting" fractions were analyzed through UV-MALDI-TOF MS together with a subfraction of the "non-interacting" material, using sinapinic acid (SA) as matrix. The spectra were obtained in linear positive mode in the 4.0-90.0 kDa mass/charge range showing peaks in well defined zones, namely: 5.5-8.0 kDa, 10.0-12.0 kDa, 12.5-14.0 kDa (major), 23.2-23.7 kDa, 26.1-27.5 kDa and 38.0-40.0 kDa. High sensitivity spectra showed some very small peaks until 90 kDa. Bovine seminal protein (BSP-A3), acidic seminal fluid protein (aSFP) and PDC-109 glycoproteins (BSP-A1 and BSP-A2) were identified. Caltrin, the human epididymis-specific glycoprotein (HE4), the calcium transport inhibitor protein, the inhibitor of metalloprotease 2 (TIMP-2), osteopontin (OPN) and the prostatic acid protease (PAP) were tentatively identified. The molecular weight of some peaks can be arranged in a sequence from that of BSP-A3 going through the molecular weights of glycoforms (including the known BSP-A1 and BSP-A2) which differ in the amounts of neutral hexoses and sialic acids, composing a BSP-family more extended than previously reported. Another two families could be builded up from proteins of molecular weight of about 12730 and 12750 Da and glycoforms which differ from them also by hexoses and sialic acids. The structures of the deduced O-linked oligosaccharides of the glycoforms are in complete agreement to that determined for the BSP-A1 Oligosaccharide. Small differences in the m. w. of some (glyco)proteins were attributed to genetic polymorphysm. The identification of proteins and O-linked glycoproteins in the "interacting" fractions of the chromatography suggests that the fractionation was not due to specific affinity interactions but to non-specific hydrophobic interactions of the proteins with the hydrophobic pocked of the Con A. Fil:Cerezo, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Giudicessi, S.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Erra-Balsells, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marquinez, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1880554X_v45_n4_p267_Cerezo http://hdl.handle.net/20.500.12110/paper_1880554X_v45_n4_p267_Cerezo
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Bovine seminal plasma
Glyco)proteins
Nor-harmane
Sinapinic acid
UV-MALDITOF MS
spellingShingle Bovine seminal plasma
Glyco)proteins
Nor-harmane
Sinapinic acid
UV-MALDITOF MS
Cerezo, Alberto Saúl
Giudicessi, Silvana Laura
Erra Balsells, Rosa
Marquínez, Ana Claudia
Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
topic_facet Bovine seminal plasma
Glyco)proteins
Nor-harmane
Sinapinic acid
UV-MALDITOF MS
description Bovine seminal plasma was submitted to chromatography on Con A-Sepharose. The "noninteracting", "weakly-interacting" and "strongly-interacting" fractions were analyzed through UV-MALDI-TOF MS together with a subfraction of the "non-interacting" material, using sinapinic acid (SA) as matrix. The spectra were obtained in linear positive mode in the 4.0-90.0 kDa mass/charge range showing peaks in well defined zones, namely: 5.5-8.0 kDa, 10.0-12.0 kDa, 12.5-14.0 kDa (major), 23.2-23.7 kDa, 26.1-27.5 kDa and 38.0-40.0 kDa. High sensitivity spectra showed some very small peaks until 90 kDa. Bovine seminal protein (BSP-A3), acidic seminal fluid protein (aSFP) and PDC-109 glycoproteins (BSP-A1 and BSP-A2) were identified. Caltrin, the human epididymis-specific glycoprotein (HE4), the calcium transport inhibitor protein, the inhibitor of metalloprotease 2 (TIMP-2), osteopontin (OPN) and the prostatic acid protease (PAP) were tentatively identified. The molecular weight of some peaks can be arranged in a sequence from that of BSP-A3 going through the molecular weights of glycoforms (including the known BSP-A1 and BSP-A2) which differ in the amounts of neutral hexoses and sialic acids, composing a BSP-family more extended than previously reported. Another two families could be builded up from proteins of molecular weight of about 12730 and 12750 Da and glycoforms which differ from them also by hexoses and sialic acids. The structures of the deduced O-linked oligosaccharides of the glycoforms are in complete agreement to that determined for the BSP-A1 Oligosaccharide. Small differences in the m. w. of some (glyco)proteins were attributed to genetic polymorphysm. The identification of proteins and O-linked glycoproteins in the "interacting" fractions of the chromatography suggests that the fractionation was not due to specific affinity interactions but to non-specific hydrophobic interactions of the proteins with the hydrophobic pocked of the Con A.
author Cerezo, Alberto Saúl
Giudicessi, Silvana Laura
Erra Balsells, Rosa
Marquínez, Ana Claudia
author_facet Cerezo, Alberto Saúl
Giudicessi, Silvana Laura
Erra Balsells, Rosa
Marquínez, Ana Claudia
author_sort Cerezo, Alberto Saúl
title Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
title_short Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
title_full Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
title_fullStr Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
title_full_unstemmed Direct UV-MALDI-TOF MS analysis of (Glyco)proteins of fractions of bovine seminal plasma
title_sort direct uv-maldi-tof ms analysis of (glyco)proteins of fractions of bovine seminal plasma
publishDate 2007
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1880554X_v45_n4_p267_Cerezo
http://hdl.handle.net/20.500.12110/paper_1880554X_v45_n4_p267_Cerezo
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