The amino acid sequence of wheat β-purothionin

1976 ◽  
Vol 54 (10) ◽  
pp. 835-842 ◽  
Author(s):  
A. S. Mak ◽  
B. L. Jones
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Basic Protein ◽  
Viscum Album ◽  
Low Molecular Weight ◽  
Amino Acid Residues ◽  
Basic Proteins ◽  
Considerable Homology

The complete amino acid sequence of β-purothionin, a low molecular weight, very basic, protein isolated from wheat endosperm material, has been determined. β-purothionin is toxic to some bacteria, to yeasts, and to animals when injected. The protein contains 45 amino acid residues and has a molecular weight of 4913. The 8 cysteine and 10 basic residues are distributed throughout the molecule. The primary structure of the protein shows considerable homology to those of the viscotoxins, which are toxic, small, basic proteins found in the leaves and stems of European mistletoe (Viscum album L.).

scholarly journals Amino acid sequence of the smaller basic protein from rat brain myelin

1974 ◽  
Vol 141 (1) ◽  
pp. 243-255 ◽  
Author(s):  
Peter R. Dunkley ◽  
Patrick R. Carnegie
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rat Brain ◽  
Basic Protein ◽  
Detailed Comparison ◽  
British Library ◽  
Amino Acid Residues ◽  
Variable Regions ◽  
Basic Proteins ◽  
Lending Library

1. The complete amino acid sequence of the smaller basic protein from rat brain myelin was determined. This protein differs from myelin basic proteins of other species in having a deletion of a polypeptide of 40 amino acid residues from the centre of the molecule. 2. A detailed comparison is made of the constant and variable regions in a group of myelin basic proteins from six species. 3. An arginine residue in the rat protein was found to be partially methylated. The ratio of methylated to unmethylated arginine at this position differed from that found for the human basic protein. 4. Three tryptic peptides were isolated in more than one form. The differences between the two forms of each peptide are discussed in relation to the electrophoretic heterogeneity of myelin basic proteins, which is known to occur at alkaline pH values. 5. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50029 at the British Library (Lending Division) (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

Amino acid sequence of the acidic acrosin inhibitor (BUSI I B2) from bull seminal plasma

1983 ◽  
Vol 48 (9) ◽  
pp. 2558-2568 ◽  
Author(s):  
Bedřich Meloun ◽  
Věra Jonáková ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Sequential Data ◽  
Amino Acid Residues

The molecule of the inhibitor consists of 63 amino acid residues whose sequence is the following: Glu-Ile-Tyr-Phe-Glu-Pro-Asp-Phe-Gly-Phe-Pro-Pro-Asp-Cys-Lys-Val-Tyr-Thr-Glu-Ala-Cys-Thr-Arg-Glu-Tyr-Asn-Pro-Ile-Cys-Asp-Ser-Ala-Ala-Lys-Thr-Tyr-Ser-Asn-Glu-Cys-Thr-Phe-Cys-Asn-Glu-Lys-Met-Asn-Asn-Asp-Ala-Asp-Ile-His-Phe-Gln-His-Phe-Gly-Glu-Cys-Glu-Tyr. The sequential data were obtained by the analysis of peptides isolated from the tryptic and chymotryptic digest of the carboxymethylated inhibitor. The molecular weight of the inhibitor calculated from its amino acid sequence is 7377.

scholarly journals The partial amino acid sequence of the major low molecular weight component of two human amyloid fibrils

FEBS Letters ◽  
1972 ◽  
Vol 22 (1) ◽  
pp. 121-123 ◽  
Author(s):  
Edward C. Franklin ◽  
Mordechai Pras ◽  
Mark Levin ◽  
Blas Frangione
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amyloid Fibrils ◽  
Low Molecular Weight ◽  
Partial Amino Acid Sequence

scholarly journals Primary Structure of Apovitellenin I From Hen Egg Yolk and its Comparison With Emu Apovitellenin I

1976 ◽  
Vol 29 (3) ◽  
pp. 175 ◽  
Author(s):  
TAA Dopheide ◽  
AS Inglis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Egg Yolk ◽  
Structure And Function ◽  
Single Base ◽  
Hen Egg Yolk ◽  
Considerable Homology ◽  
And Function ◽  
Hen Egg

The amino acid sequence of apovitellenin I from hen egg yolk has been determined using both automatic and manual procedures; it comprises 82 residues. Hen apovitellenin shows considerable homology with emu apovitellenin I which contains 84 residues. Besides two deletions in the sequence, the hen protein differs in 28 positions from the emu protein; 26 of these positions may have arisen from single base changes. The changes are largely conservative ones, which suggest that the structure and function have been preserved despite extensive mutation.

scholarly journals Isolation and amino acid sequence of a short-chain neurotoxin from an Australian elapid snake, Pseudechis australis

1985 ◽  
Vol 232 (2) ◽  
pp. 367-371 ◽  
Author(s):  
C Takasaki ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Short Chain ◽  
Amino Acid Residues ◽  
Sea Snakes ◽  
Considerable Homology

A short-chain neurotoxin Pseudechis australis a (toxin Pa a) was isolated from the venom of an Australian elapid snake Pseudechis australis (king brown snake) by sequential chromatography on CM-cellulose, Sephadex G-50 and CM-cellulose columns. Toxin Pa a has an LD50 (intravenous) value of 76 micrograms/kg body wt. in mice and consists of 62 amino acid residues. The amino acid sequence of Pa a shows considerable homology with those of short-chain neurotoxins of elapid snakes, especially of true sea snakes.

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