2018
DOI: 10.4172/2161-1009.1000351
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Identification of Major Proteins of a Very Stable High Molecular Mass Multi-Protein Complex of Human Placental Tissue Possessing Nine Different Catalytic Activities

Abstract: Human placenta is an organ protecting, feeding, and regulating the grooving of the embryo. Therefore, identification and characterization of placental components including proteins and their multi-protein complexes is an important step to understanding the placenta function. Here we analyzed for the first time human placentas extremely stable multi-protein complex (SPC, ~1000 kDa) by MALDI MS and MS/MS spectrometry using proteins tryptic hydrolyzates after proteins separation by SDS-PAGE and 2-D electrophoresi… Show more

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Cited by 5 publications
(31 citation statements)
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“…Milk is more than a source of nutrients and vitamins for newborn [99]; it contains different proteins and protein complexes [100] with very diverse functions. Milk is a biological liquid containing vesicles of different size and shapes.…”
Section: Discussionmentioning
confidence: 99%
“…Milk is more than a source of nutrients and vitamins for newborn [99]; it contains different proteins and protein complexes [100] with very diverse functions. Milk is a biological liquid containing vesicles of different size and shapes.…”
Section: Discussionmentioning
confidence: 99%
“…Different biological fluids contain various high molecular weight aggregates of multiple proteins co-isolated with exosomes under different centrifugations. Human placenta was shown to contain an extremely stable multiprotein complex (~1000 kDa), with sizes comparable to exosomes [ 64 ]. This complex possesses nine different catalytic activities: DNase, RNase, ATPase, phosphatase, protease, amylase, catalase, peroxidase (H 2 O 2 -dependent), and oxidoreductase (H 2 O 2 -independent).…”
Section: Methods Of Exosome Isolationmentioning
confidence: 99%
“…The possibility of the existence of multi-protein complexes in the soluble fraction of a homogenate of human milk [ 9 ], placenta [ 10 , 11 ], and eggs of sea urchins [ 12 ] was recently analyzed. The extremely stable complexes of different proteins (≈1000 ± 100 kDa) were isolated from milk, placentas, and eggs of sea urchins by FPLC gel filtration [ 9 , 10 , 11 , 12 ]. These three protein complexes were stable in the presence of MgCl 2 and NaCl in high concentrations.…”
Section: Introductionmentioning
confidence: 99%
“…These three protein complexes were stable in the presence of MgCl 2 and NaCl in high concentrations. All complexes were dissociated only in the presence of 8 M urea + 1.0–3.0 M NaCl, or MgCl 2 [ 9 , 10 , 11 , 12 ]. In the case of the placentas, milk, and eggs of sea urchins, the stable complexes, according to SDS-PAGE, contain several, yet different proteins having molecular masses (MMs) from 14 to 79.3 kDa [ 9 , 10 , 11 , 12 ].…”
Section: Introductionmentioning
confidence: 99%
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