Isolation and characterization of β-lipolytic hormone from porcine pituitary gland

1970 ◽  
Vol 48 (9) ◽  
pp. 1017-1021 ◽  
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Pituitary Gland ◽  
Amino Acid Composition ◽  
Biological Activities ◽  
Terminal Amino Acid ◽  
Isolation And Characterization ◽  
Pituitary Glands ◽  
Terminal Amino

A lipolytic substance was isolated from porcine pituitary glands. It's amino acid composition, molecular weight, N-terminal amino acid, isoelectric point, and biological activities are reported. These results are compared to the corresponding values of sheep β-lipolytic hormone.

IMPROVED PROCEDURES FOR PREPARATION AND CHARACTERIZATION OF MYROTHECIUM CELLULASE: PART 3. MOLECULAR WEIGHT, AMINO ACID COMPOSITION, TERMINAL RESIDUES, AND OTHER PROPERTIES

1963 ◽  
Vol 41 (3) ◽  
pp. 697-705 ◽  
Author(s):  
P. K. Datta ◽  
K. R. Hanson ◽  
D. R. Whitaker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Fingerprint Pattern ◽  
Sulphydryl Groups ◽  
Terminal Amino

The molecular weight of Myrothecium cellulase was estimated by the Archibald method to be approximately 49,000. No N-terminal amino acid could be detected by the Edman degradation or with fluorodinitrobenzene. Hydrazinolysis gave glycine as the C-terminal amino acid. No free sulphydryl groups could be detected in the enzyme. The amino acid composition and the fingerprint pattern after tryptic digestion were determined.

IMPROVED PROCEDURES FOR PREPARATION AND CHARACTERIZATION OF MYROTHECIUM CELLULASE: PART 3. MOLECULAR WEIGHT, AMINO ACID COMPOSITION, TERMINAL RESIDUES, AND OTHER PROPERTIES

1963 ◽  
Vol 41 (1) ◽  
pp. 697-705 ◽  
Author(s):  
P. K. Datta ◽  
K. R. Hanson ◽  
D. R. Whitaker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Fingerprint Pattern ◽  
Sulphydryl Groups ◽  
Terminal Amino

The molecular weight of Myrothecium cellulase was estimated by the Archibald method to be approximately 49,000. No N-terminal amino acid could be detected by the Edman degradation or with fluorodinitrobenzene. Hydrazinolysis gave glycine as the C-terminal amino acid. No free sulphydryl groups could be detected in the enzyme. The amino acid composition and the fingerprint pattern after tryptic digestion were determined.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

Physikalische, chemische und biologische Charakterisierung von menschlichem Choriongonadotropin

1968 ◽  
Vol 23 (11) ◽  
pp. 1412-1426 ◽  
Author(s):  
H. D. Schlumberger
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Biological Activities ◽  
Guanidine Hydrochloride ◽  
Group Analysis ◽  
Residual Activity ◽  
Apparent Molecular Weight ◽  
Terminal Amino Acid ◽  
Original Activity ◽  
Terminal Amino

Purification of commercially available HCG preparations with DEAE Sephadex A 50 and Sephadex G 100 column chromatography gave homogeneous fractions having specific biological activities four fold those of the starting materials. The purified HCG has ICSH characteristics and, in high doses, a definite FSH effect is present.Chemical analysis of HCG showed it to contain 29% carbohydrates and 69% peptides. The C-terminal amino acid of the peptide chain was found to be serine, but the N-terminal amino acid could not be determined with normal methods. A molecular weight of 22000 — 27000 daltons was obtained by quantitative end group analysis. Ultracentrifugation experiments in 4 m guanidine hydrochloride gave a molecular weight of 27200 daltons, but in neutral saline solutions at HCG concentrations above 2 mg/ml the apparent molecular weight was higher and indicated dimer formation. A dissociation constant of 10-5 mol/l was estimated for the monomer-dimer equilibrium. Since biological activity is found with 0.1 to 0.5 µg, it was concluded that the HCG monomer is the active entity.The purified HCG is stable from pH 4.5 to pH 10 for 6 hours at 37 °C. At pH 2.5 only 5 to 10% of the original activity is retained. HCG is rapidly inactivated at 100 °C, but a residual activity of 6 — 10% remained after 30 minutes at 80 °C. No activity was lost after 30 minutes incubation at 60 °C.

Purification and partial chemical characterization of human pituitary lipolytic hormone

1976 ◽  
Vol 54 (9) ◽  
pp. 778-782 ◽  
Author(s):  
M. Chrétien ◽  
C. Gilardeau ◽  
N. Seidah ◽  
M. Lis
Keyword(s):  
Amino Acid ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Human Pituitary ◽  
Leucine Residue ◽  
N Terminus ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical

Frozen human pituitary glands contain a lipotropic hormone which is similar to but not identical with ovine, bovine, and porcine beta-lipotropin. Six of the first seven residues from the N-terminus are [Formula: see text] The C-terminal amino acid is a leucine residue.

scholarly journals PHYSICOCHEMICAL CHARACTERIZATION OF PITUITARY FOLLICLE-STIMULATING HORMONE

1952 ◽  
Vol 35 (4) ◽  
pp. 629-637 ◽  
Author(s):  
Choh Hao Li ◽  
Kai O. Pedersen
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Follicle Stimulating Hormone ◽  
Physicochemical Characterization ◽  
Single Protein ◽  
Pituitary Glands ◽  
The Stability ◽  
Stimulating Hormone

The physiochemical characteristics of the follicle-stimulating hormone (FSH) from whole sheep pituitary glands have been studied. The hormone behaves as a single protein in electrophoresis, diffusion, and ultracentrifugation. It has an isoelectric point at pH 4.5 and a molecular weight of 67,000 and contains 1.23 per cent hexose and 1.51 per cent hexosamine. The amino acid composition has also been determined in large part. The stability of the hormone to acid and heat has been investigated.

scholarly journals Characterization of gastric mucoproteins isolated by equilibrium density-gradient centrifugation in caesium chloride

1974 ◽  
Vol 141 (3) ◽  
pp. 633-639 ◽  
Author(s):  
Bryan J. Starkey ◽  
David Snary ◽  
Adrian Allen
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gradient Centrifugation ◽  
Gel Filtration ◽  
Equilibrium Density ◽  
Amino Acid Residues ◽  
Gastric Mucus ◽  
Terminal Amino Acid ◽  
Terminal Amino

1. The mucoprotein from pig gastric mucus has been purified by equilibrium centrifugation in a CsCl gradient. 2. This procedure removes the non-covalently bound protein, which is closely associated with the mucoprotein and not easily removed from it by gel filtration. 3. The purified mucoprotein is separable by gel filtration into a high-molecular-weight mucoprotein A (mol.wt. 2.3×106) and a low-molecular-weight mucoprotein B/C (mol.wt. 1.15×106). 4. These two mucoproteins have the same chemical analysis namely fucose 11.3%, galactose 26%, glucosamine 19.5%, galactosamine 8.3% and protein 13.6%. 5. Mucoprotein A contains 3.1% ester sulphate. 6. These mucoproteins are isolated without enzymic digestion and have a higher protein content than the blood-group-substance mucoproteins from proteolytic digestion of gastric mucus. Detailed amino acid analysis shows that the extra protein in the non-enzymically digested material is composed of amino acids other than serine and threonine. 7. Mucoproteins A and B/C contain respectively 130 and 9 half-cystine residues per molecule of which about 78 and 6 residues are involved in disulphide linkages. 8. Cleavage of these disulphide linkages by mercaptoethanol splits both mucoproteins into four equally sized subunits of mol.wt. 5.2×105for mucoprotein A and 2.8×104for mucoprotein B/C. 9. The sole N-terminal amino acid of mucoprotein A is aspartic acid, whereas mucoprotein B/C has several different N-terminal amino acid residues.

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