Acid Proteases from Species of Mucor. II. Partial Characterization of the Acid Protease Produced by a Strain of Mucor miehei Isolated in Cuba

1975 ◽  
Vol 53 (3) ◽  
pp. 269-274 ◽  
Author(s):  
W. S. Rickert ◽  
P. A. McBride-Warren
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Detailed Comparison ◽  
Acid Protease ◽  
Total Carbohydrate ◽  
Mucor Miehei ◽  
Total Carbohydrate Content ◽  
Helical Content

The acid protease produced by a strain of Mucor miehei isolated in Cuba was purified by column electrofocusing and partially characterized as to amino-acid composition, molecular weight, helical content, total carbohydrate content, and approximate isoelectric point. A detailed comparison of these results with those reported previously for Mucor miehei protease (Ottesen, M. &Rickert, W. S. (1970) C.R. Trav. Lab. Carlsberg 37, 301) suggested that the two enzymes are similar but not identical. This conclusion was reinforced by an analysis of circular-dichroism spectra.

Acid Proteases From Species of Mucor: Molecular Weight of Mucor miehei Protease From Amino Acid Analysis Data

1973 ◽  
Vol 51 (12) ◽  
pp. 1638-1646 ◽  
Author(s):  
W. S. Rickert ◽  
J. R. Elliott
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Weight Function ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Analysis ◽  
Analysis Data ◽  
Improved Method ◽  
Mucor Miehei ◽  
A Value

An improved method for the isolation of Mucor miehei protease which utilizes a diafiltration cell has been used to obtain a highly purified protein in gram quantities and yields of about 80%. Based on a modified molecular weight function and data from amino acid analysis, a value of 41 800 for the molecular weight of the glycoprotein was established and some modification to the published amino acid composition was made. These results suggest that Mucor miehei protease is distinctly different from the two other acid proteases which are also produced by species of Mucor.

Extraction and Characterization of Galactomannan from Seeds of Leucaena leucocephala

2015 ◽  
Vol 1134 ◽  
pp. 213-219 ◽  
Author(s):  
Shazlinda Shirajuddin ◽  
Dzaraini Kamarun ◽  
Nahlah Elkudssiah Ismail ◽  
Mohd Shahezwan Abdul Wahab ◽  
Abdul Rashid Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nuclear Magnetic Resonance ◽  
High Performance Liquid Chromatography ◽  
Leucaena Leucocephala ◽  
High Performance ◽  
Drug Carrier ◽  
Total Carbohydrate ◽  
Total Carbohydrate Content ◽  
G Ratio

Galactomannan is a biopolymer polysaccharides mostly obtained from Leguminosae plant have shown an interesting capability as drug carrier. In this study, galactomannan from the seeds ofLeucaenaleucocephalaknown locally as ‘petai belalang’ was obtained by water extraction. The galactomannan was characterized structurally by nuclear magnetic resonance (NMR) and fourier transform infrared spectroscopy (FTIR). Highly molecular weight of galactomannan, > 2.56 x 106Da, was successfully extracted from the plant. Total carbohydrate content of this polysaccharides is 74.84% and composition of galactose and mannose have been confirm by high performance liquid chromatography (HPLC) which is 36.67% and 38.17% respectively. M/G ratio was determined as 1:1. Hence, galactomannan has been successfully extracted from the seeds ofLeucaenaleucocephala.

scholarly journals High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

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.

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 The purification in high yield and characterization of rat hepatic glucokinase

1976 ◽  
Vol 153 (2) ◽  
pp. 363-373 ◽  
Author(s):  
M J Holroyde ◽  
M B Allen ◽  
A C Storer ◽  
A S Warsy ◽  
J M E Chesher ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Affinity Chromatography ◽  
Amino Acid Composition ◽  
Specific Activity ◽  
Sedimentation Equilibrium ◽  
High Yield ◽  
Equilibrium Studies ◽  
Enzyme Specific Activity

A new improved procedure for the purification of rat hepatic glucokinase (ATP-d-glucose 6-phosphotransferase, EC 2.7.1.2) is given. A key step is affinity chromatography on Sepharose-N-(6-aminohexanoyl)-2-amino-2-deoxy-d-glucopyranose. A homogeneous enzyme, specific activity 150 units/mg of protein, is obtained in about 40% yield. The molecular weight of the pure enzyme was determined by several procedures. In particular, sedimentation-equilibrium studies under a variety of conditions indicate a molecular weight of 48000 and no evidence for dimerization; reports in the literature of other values are discussed in the light of this evidence on the pure enzyme. The amino acid composition suggests that hepatic glucokinase is closely related to rat brain hexokinase and also the wheat “light” hexokinases.

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.

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