Identification of mare colostrum proteins

Colostrum is an essential feed of foals. It is a source of nutrients and functional proteins significant for foals’ growth and development. In the presented research using two-dimensional electrophoresis coupled via spectrometry mass MALDI-TOF in the mares’ colostrum (whey proteins fraction) were identified 24 proteins representing 15 different gene products. The identified proteins were involved in supporting foals’ immature immune systems and in the transport of various compounds. Further research of mares’ colostrum will allow determining more gene products. An in-depth analysis of mares’ milk will provide information about biochemical processes occurring in the mammary gland of the mare during the lactation period.

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"Map" of proteins resolved from human chorionic villi by two-dimensional electrophoresis.

Clinical Chemistry ◽

10.1093/clinchem/30.12.2040 ◽

1984 ◽

Vol 30 (12) ◽

pp. 2040-2042 ◽

Cited By ~ 1

Author(s):

P L Trnka ◽

E Pergament ◽

N G Anderson

Keyword(s):

Cell Types ◽

First Trimester ◽

Gene Products ◽

Two Dimensional ◽

Chorionic Villi ◽

Two Dimensional Electrophoresis ◽

Chorionic Plate ◽

Reference Map ◽

Dimensional Electrophoresis ◽

Fetal Genotype

Abstract Two-dimensional electrophoresis was applied to specimens of human chorionic villi obtained during the first trimester of gestation, the object being to simultaneously map several hundred polypeptide gene products. Genetically normal specimens were homogenized in a urea-based denaturant and the supernates were electrophoresed with use of the "ISO-DALT" system. Four categories of proteins are distinguished on the map: previously identified proteins present in chorionic villi and other cell types; unidentified proteins present in chorionic villi and other cell types; proteins present in chorionic villi and amniotic fluid but not in other cell types; and proteins probably originating from the amnio-chorionic plate. The reference map for chorionic villi provided in this study may serve as the basis of determining whether genetic analyses conducted in the first trimester accurately represent the fetal genotype.

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The Identification Maps and Developmental Changes of Horse Milk Proteins in Lactation Period by Microscale Multisample Two-dimensional Electrophoresis

Nihon Chikusan Gakkaiho ◽

10.2508/chikusan.60.450 ◽

1989 ◽

Vol 60 (5) ◽

pp. 450-458 ◽

Cited By ~ 1

Author(s):

Michinari YOKOHAMA ◽

Takashi AMANO ◽

Kazushige MOGI

Keyword(s):

Milk Proteins ◽

Developmental Changes ◽

Lactation Period ◽

Two Dimensional ◽

Two Dimensional Electrophoresis ◽

Dimensional Electrophoresis

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Identification of wallaby milk whey proteins separated by two-dimensional electrophoresis, using amino acid analysis and sequence tagging

Electrophoresis ◽

10.1002/elps.1150180708 ◽

1997 ◽

Vol 18 (7) ◽

pp. 1073-1078 ◽

Cited By ~ 15

Author(s):

Mark P. Molloy ◽

Ben R. Herbert ◽

Jun X. Yan ◽

Keith L. Williams ◽

Andrew A. Gooley

Keyword(s):

Amino Acid ◽

Amino Acid Analysis ◽

Whey Proteins ◽

Two Dimensional ◽

Milk Whey ◽

Two Dimensional Electrophoresis ◽

Dimensional Electrophoresis

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Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657116 ◽

1982 ◽

Vol 47 (01) ◽

pp. 019-021 ◽

Cited By ~ 13

Author(s):

Cemal Kuyas ◽

André Haeberli ◽

P Werner Straub

Keyword(s):

Sialic Acid ◽

Polypeptide Chain ◽

Two Dimensional ◽

Charge Heterogeneity ◽

Human Fibrinogen ◽

Two Dimensional Electrophoresis ◽

Isoelectric Points ◽

Polypeptide Chains ◽

Dimensional Electrophoresis ◽

Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

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