Large-scale preparation of sialyl-Tn antigen-containing peptides from mucin-like glycoproteins in boar seminal gel

2021 ◽  
Author(s):  
Ryota Takeuchi ◽  
Megumi Maeda ◽  
Miran Nakano ◽  
Hiroaki Funahashi ◽  
Yoshinobu Kimura
Keyword(s):  
Tumor Antigen ◽  
Large Scale ◽  
Gel Filtration ◽  
New Method ◽  
Tn Antigen ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Sialyl Tn Antigen ◽  
Unused Resource ◽  
Sialyl Tn

Abstract Sialyl-Tn antigen, a tumor antigen, is a valuable ligand for the purification of proteins that specifically bind to it. Here, we developed a new method for the preparation of large amounts of sialyl-Tn antigen-containing peptides from an unused resource, boar seminal gel. The glycopeptides were prepared from the actinase E digests by a combination of gel filtration and hydrophilic partitioning.

Purification of the Antihemophilic Factor by Gel Filtration on Agarose

1969 ◽  
Vol 22 (03) ◽  
pp. 577-583 ◽  
Author(s):  
M.M.P Paulssen ◽  
A.C.M.G.B Wouterlood ◽  
H.L.M.A Scheffers
Keyword(s):  
Factor Viii ◽  
Plasma Proteins ◽  
Large Scale ◽  
Gel Filtration ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Antihemophilic Factor

SummaryFactor VIII can be isolated from plasma proteins, including fibrinogen by chromatography on agarose. The best results were obtained with Sepharose 6B. Large scale preparation is also possible when cryoprecipitate is separated by chromatography. In most fractions containing factor VIII a turbidity is observed which may be due to the presence of chylomicrons.The purified factor VIII was active in vivo as well as in vitro.

scholarly journals Ostrich crystallins. Structural characterization of δ-crystallin with enzymic activity

1991 ◽  
Vol 273 (2) ◽  
pp. 295-300 ◽  
Author(s):  
S H Chiou ◽  
C H Lo ◽  
C Y Chang ◽  
T Itoh ◽  
H Kaji ◽  
...  
Keyword(s):  
Large Scale ◽  
Gel Filtration ◽  
Helical Structure ◽  
Enzymic Activity ◽  
Lens Crystallins ◽  
Large Scale Preparation ◽  
Helical Content ◽  
Lyase Activity ◽  
Molecular Masses ◽  
Scale Preparation

Lens crystallins from the African ostrich (Struthio camelus) were isolated and characterized. Four crystallin fractions corresponding to alpha-, delta/beta- and beta-crystallins similar to those of duck crystallins were isolated, but epsilon-crystallin was found to be absent. The native molecular masses and subunit structures of the purified fractions were analysed by gel filtration. SDS/PAGE and isoelectric focusing, revealing various extents of heterogeneity in each orthologous crystallin class. An ion-exchange chromatographic method was used for the large-scale preparation of delta-crystallin suitable for structural and enzymic studies. It was unexpectedly found that the purified native delta-crystallin of ostrich lens possessed high argininosuccinate lyase activity, in contrast with chicken delta-crystallin. The c.d. spectra indicated a predominant beta-sheet structure in alpha- and beta-crystallins, and a significant contribution of alpha-helical structure in the delta-crystallin fraction. The estimate of secondary structures from c.d. spectroscopy for each crystallin class bears a resemblance to that of duck crystallins, except that ostrich delta-crystallin possesses much less helical content than duck delta-crystallin. Comparison of crystallin compositions and structures from aquatic and terrestrial birds revealed distinct differences.

scholarly journals New Method for Large-Scale Preparation of Covalently Closed λ DNA Molecules

1974 ◽  
Vol 14 (5) ◽  
pp. 1104-1107 ◽  
Author(s):  
R. Reuben ◽  
M. Gefter ◽  
L. Enquist ◽  
A. Skalka
Keyword(s):  
Large Scale ◽  
New Method ◽  
Dna Molecules ◽  
Large Scale Preparation ◽  
Scale Preparation
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