scholarly journals Comparative biochemical analysis of lectin and nuclease from Chelidonium majus L.

2000 ◽  
Vol 47 (2) ◽  
pp. 413-420 ◽  
Author(s):  
E Fik ◽  
M Dalgalarrondo ◽  
T Haertlé ◽  
A Goździcka-Józefiak
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Biochemical Analysis ◽  
Dnase Activity ◽  
Chelidonium Majus ◽  
Terminal Sequence ◽  
Leaves And Roots ◽  
Comparative Biochemical Analysis

It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Goździcka-Józefiak & Kedzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24 kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.

scholarly journals Amino Acid Composition and Amino-Terminal Sequence of Yeast Enolase

1959 ◽  
Vol 234 (5) ◽  
pp. 1108-1111
Author(s):  
Bo G. Malmström ◽  
J.R. Kimmel ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Yeast Enolase

scholarly journals Silkmoth chorion proteins. Their diversity, amino acid composition, and the NH-terminal sequence of one component

1978 ◽  
Vol 253 (4) ◽  
pp. 1305-1314
Author(s):  
J.C. Regier ◽  
F.C. Kafatos ◽  
K.J. Kramer ◽  
R.L. Heinrikson ◽  
P.S. Keim
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Silkmoth Chorion

Proteins in the Enamel Fluid of Immature Porcine Teeth

1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Permanent Teeth ◽  
Major Protein ◽  
Protein Species ◽  
Terminal Sequence ◽  
Molecular Weights ◽  
Sds Electrophoresis

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.

Determination of the N-terminal sequence and amino acid composition of MM and BB isozymes of porcine creatine phosphokinase

1988 ◽  
Vol 106 (3) ◽  
pp. 1250-1252
Author(s):  
F. E. Romantsev ◽  
V. N. Prozorovskii ◽  
A. A. Rzhaninova ◽  
E. L. Trebukhina
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Creatine Phosphokinase ◽  
Terminal Sequence

Ovine lactoferrin: isolation from colostrum and characterization

1991 ◽  
Vol 58 (2) ◽  
pp. 211-218 ◽  
Author(s):  
Richard Buchta
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Sds Page ◽  
C 50 ◽  
Blue Sepharose

SummaryHighly purified lactoferrin was isolated from ovine colostrum by sequential purification on CM-Sephadex C-50 and Blue-Sepharose, with overall yield of 55%. The ovine lactoferrin was characterized by SDS-PAGE, its amino acid composition and N-terminal sequence to residue 30. Homology with bovine and human lactoferrins was greater than 80 and 50% respectively. Antibodies to ovine lactoferrin were raised in rabbits and used to develop an enzyme-linked immuno-sorbent assay (ELISA). The antiserum was not cross reactive with other colostrum proteins.

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