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.

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.

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.

scholarly journals Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva

1991 ◽  
Vol 280 (2) ◽  
pp. 341-352 ◽  
Author(s):  
N Ramasubbu ◽  
M S Reddy ◽  
E J Bergey ◽  
G G Haraszthy ◽  
S D Soni ◽  
...  
Keyword(s):  
Large Scale ◽  
Guanidine Hydrochloride ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Proline Rich Peptide ◽  
Purification Protocol

The major components of human submandibular-sublingual saliva (HSMSL) are mucins, amylases, cystatins, proline-rich proteins and statherin. Structure-function studies of these molecules have been hampered by the small amounts of purified materials that can be isolated from human secretions. The present study describes an integrated purification protocol for the large-scale preparation of many of these molecules. To dissociate partially heterotypic complexes among salivary molecules, HSMSL was initially fractionated into four pools by gel filtration with 6 M-guanidine hydrochloride. Subsequent fractionation of these four pools by gel-filtration and ion-exchange chromatography resulted in the purification of high- and low-Mr mucins, neutral and acidic cystatins, acidic and basic proline-rich proteins and statherin. Many variants or isoforms of these salivary molecules have been identified and biochemically characterized. Biochemical studies indicated that the low-Mr mucin exists as two isoforms which vary in their sialic acid to fucose ratios. Three isoforms of acidic cystatin S were characterized which differ in their phosphate content. Two isoforms of a basic proline-rich peptide were identified; the smaller peptide was a truncated form missing the first seven amino acids.

LARGE-SCALE PREPARATION OF HIGHLY PURIFIED PYROGEN-FREE HUMAN GROWTH HORMONE FOR CLINICAL USE

1979 ◽  
Vol 82 (1) ◽  
pp. 77-86 ◽  
Author(s):  
R. LUMLEY JONES ◽  
G. BENKER ◽  
P. R. SALACINSKI ◽  
T. J. LLOYD ◽  
P. J. LOWRY
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Large Scale ◽  
Gel Filtration ◽  
Human Growth ◽  
Exchange Chromatography ◽  
Large Scale Preparation ◽  
Alkaline Conditions ◽  
Pituitary Glands ◽  
Scale Preparation

SUMMARY A method is described for the large-scale isolation of highly purified human growth hormone for therapeutic use. The hormone was extracted from frozen pituitary glands under mildly alkaline conditions. Purification was effected by gel filtration and ion-exchange chromatography. The final product was pyrogen-free and had a potency of 2·5 i.u./mg measured by bioassay against the current international standard. The yield of growth hormone/gland was approximately 5 mg.

The occurrence of long chain polyprenols in leaves of plants of Rosaceae family and their isolation by time-extended liquid chromatography

1992 ◽  
Vol 70 (6) ◽  
pp. 448-454 ◽  
Author(s):  
Ewa Świeżewska ◽  
T. Chojnacki ◽  
W. J. Jankowski ◽  
K. Singh ◽  
J. Olsson
Keyword(s):  
Liquid Chromatography ◽  
Fatty Acid ◽  
Large Scale ◽  
Fatty Acid Esters ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Wet Weight ◽  
Rosaceae Family ◽  
Acid Esters ◽  
Long Chain

The long chain polyprenols composed of 30 and more isoprene units from leaves of plants belonging to the genera Potentilla and Rosa have been described. They occur in the form of fatty acid esters. The composition of polyprenol mixture was species dependent and its content reached ca. 0.5% wet weight. Large scale preparation of individual polyprenols from a natural polyprenol mixture was performed using time-extended liquid chromatography on the hydrophobic gel Lipidex-5000.Key words: long chain polyprenols, Rosaceae.

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