Amino acid sequence of basic acrosin inhibitor from bull seminal plasma

1979 ◽  
Vol 44 (9) ◽  
pp. 2710-2721 ◽  
Author(s):  
Bedřich Meloun ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Carboxylic Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Terminal Group ◽  
Sequential Data ◽  
Amino Acid Residues ◽  
Pyrrolidone Carboxylic Acid

The molecule of the inhibitor contains 57 amino acid residues whose sequence is the following: Pyr-Gly-Ala-Gln-Val-Asp-Cys-Ala-Glu-Phe-Lys-Asp-Pro-Lys-Val-Tyr-Cys-Thr-Arg-His-Ser-Asp-Pro-Gln-Cys-Gly-Ser-Asn-Gly-Glu-Thr-Tyr-Gly-Asn-Lys-Cys-Ala-Phe-Cys-Lys-Ala-Val-Met-Lys-Ser-Gly-Gly-Lys-Ile-Asn-Leu-Lys-His-Arg-Gly-Cys-Lys. The N-terminal group of the inhibitor is pyrrolidone carboxylic acid. The sequential data were obtained by analyses of peptides isolated from tryptic and chymotryptic digests of the oxidized or carboxymethylated inhibitor. The molecular weight of the inhibitor is 6 200.

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 Amino acid sequence of the N-terminal 108 amino acid residues of the B chain of subcomponent C1q of the first component of human complement

1978 ◽  
Vol 173 (3) ◽  
pp. 863-868 ◽  
Author(s):  
K B Reid ◽  
E O Thompson
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Amino Acid Sequence ◽  
Disulphide Bond ◽  
Amino Acid Residues ◽  
Human Complement ◽  
Terminal Amino Acid ◽  
Exact Position ◽  
Terminal Amino

The amino acid sequence of the N-terminal 108 residues of the B chain of subcomponent C1q of the first component of human complement was determined. The B chain has a blocked N-terminal amino acid, which was judged to be 5-oxopyrrolidine-2-carboxylic acid. A collagen-like region of 84 residues was found, which started at position B-6, and all of the six hydroxylysine residues and 12 hydroxyproline residues present in the chain were found in this region. Four of the six hydroxylysine residues may be glycosylated. The repeating nature of the collagen-like region is broken at position B-9, where alanine is found in a position where glycine would be expected. The exact position of the interchain disulphide bond joining the A and B chains of human subcomponent C1q was shown to be between residues A4 and B4.

scholarly journals Amino acid sequences around the cysteine residue of calf lens α-crystallin

1971 ◽  
Vol 124 (1) ◽  
pp. 61-67 ◽  
Author(s):  
P. H. Corran ◽  
S. G. Waley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Radioactive Sodium ◽  
Group 2

1. Calf lens α-crystallin was carboxymethylated with radioactive sodium iodoacetate to label the thiol group. 2. The protein was then digested with trypsin or alternatively fractionated in urea to obtain the acidic (A) chains, which were then digested with trypsin. Either procedure gave two radioactive peptides containing carboxymethylcysteine. 3. These two peptides were closely related: the longer form contained 28 amino acid residues, and the shorter lacked two residues at the N-terminal end of the longer form. 4. The amino acid sequence of the peptides have been determined. 5. No evidence for the presence of more than one cysteine residue/chain was found. 6. The question of the molecular weight of the chains is discussed.

scholarly journals MATLAB software for extracting protein name and sequence information from FASTA formatted proteome file

2019 ◽  
Author(s):  
Wenfa Ng
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Sequence Information ◽  
Amino Acid Residues ◽  
Protein Database ◽  
Matlab Software ◽  
Amino Acid Sequence Information ◽  
New Protein

FASTA file format is a common file type for distributing proteome information, especially those obtained from Uniprot. While MATLAB could automatically read fasta files using the built-in function, fastaread, important information such as protein name and organism name remain enmeshed in a character array. Hence, difficulty exists in automatic extraction of protein names from fasta proteome file to help in building a database with fields comprising protein name and its amino acid sequence. The objective of this work was in developing a MATLAB software that could automatically extract protein name and amino acid sequence information from fasta proteome file and assign them to a new database that comprises fields such as protein name, amino acid sequence, number of amino acid residues, molecular weight of protein and nucleotide sequence of protein. Information on number of amino acid residues came from the use of the length built-in function in MATLAB analyzing the length of the amino acid sequence of a protein. The final two fields were provided by MATLAB built-in functions molweight and aa2nt, respectively. Molecular weight of proteins is useful for a variety of applications while nucleotide sequence is essential for gene synthesis applications in molecular cloning. Finally, the MATLAB software is also equipped with an error check function to help detect letters in the amino acid sequence that are not part of the family of 20 natural amino acids. Sequences with such letters would constitute as error inputs to molweight and aa2nt, and would not be processed. Collectively, given that important information such as protein name is enmeshed in a character array in fasta proteome file, this work sets out to develop a MATLAB software that could automatically extract protein name and amino acid sequence information, and assigns them to a new protein database. Using built-in functions, number of amino acid residues, molecular weight and nucleotide sequence of each protein were calculated; thereby, yielding a new protein database with improved functionalities that could support a variety of biology workflows ranging from sequence alignment to molecular cloning.

scholarly journals The amino acid sequence of troponin I from rabbit skeletal muscle

1975 ◽  
Vol 149 (2) ◽  
pp. 493-496 ◽  
Author(s):  
J M Wilkinson ◽  
R J A. Grand
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Troponin I ◽  
Rabbit Skeletal Muscle ◽  
British Library ◽  
Amino Acid Residues ◽  
N Terminus

The complete amino acid sequence of rabbit skeletal muscle troponin I was determined by the isolation of the cyanogen bromide fragments and the tryptic methionine-containing peptides. Troponin I contains 179 amino acid residues and has a molecular weight of 20864. Its N-terminus is acetylated. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50055 (23 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

Disulfide bonds of basic acrosin inhibitor (BUSI II) from bull seminal plasma

1984 ◽  
Vol 49 (5) ◽  
pp. 1204-1210 ◽  
Author(s):  
Alena Rzavská ◽  
Bedřich Meloun ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Disulfide Bonds ◽  
Cysteine Residues ◽  
Chromatographic Techniques

The thermolysin digest of the basic acrosin inhibitor (molecular weight 6 200) was resolved on a column of Sephadex G-15 and subsequently by electrophoretic and chromatographic techniques. Cysteine peptides, which link together half-cysteine residues 7 and 39, 17 and 36, and 25 and 57 by disulfide bonds, were isolated. The structure of the molecule of the basic acrosin inhibitor corresponds to structures of inhibitors of the Kazal type. The amino acid sequence of a few residues in the basic acrosin inhibitor has been revised.

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.).

Thermitase from Thermoactinomyces vulgaris; amino acid sequence of the large N-terminal cyanogen bromide peptide

1985 ◽  
Vol 50 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Bedřich Meloun ◽  
Miroslav Baudyš ◽  
Manfred Pavlík ◽  
Vladimír Kostka ◽  
Gert Hausdorf ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
High Performance ◽  
Cyanogen Bromide ◽  
Sequential Data ◽  
Amino Acid Residues ◽  
Methionine Residue ◽  
Large N ◽  
Thermoactinomyces Vulgaris

The large cyanogen bromide fragment (CB1) represents the N-terminal part of the molecule of thermitase and contains 226 amino acid residues. Its molecular weight calculated from sequential data is 22 932 (the C-terminal residue is regarded as a methionine residue in the calculations). The amino acid sequence of fragment CB1 was determined by analysis of peptides obtained by tryptic hydrolysis of the fragment; these data were complemented by sequence analysis of the chymotryptic digest of fragment Mf (residues 75 through 226) and of chymotryptic fragment ET3 (residues 103 through 226) isolated from the limited tryptic digest of fragment CB1. The peptides were purified by high performance liquid chromatography and by thin layer techniques. The sequence analysis of the large peptides was effected in the sequenator, small peptides were sequenced manually by the DABITC/PITC double coupling technique. The results obtained in this study together with those of previous work5 permitted the complete amino acid sequence of fragment CB1 to be determined.

scholarly journals MATLAB software for extracting protein name and sequence information from FASTA formatted proteome file

2019 ◽  
Author(s):  
Wenfa Ng
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Sequence Information ◽  
Amino Acid Residues ◽  
Protein Database ◽  
Matlab Software ◽  
Amino Acid Sequence Information ◽  
New Protein

FASTA file format is a common file type for distributing proteome information, especially those obtained from Uniprot. While MATLAB could automatically read fasta files using the built-in function, fastaread, important information such as protein name and organism name remain enmeshed in a character array. Hence, difficulty exists in automatic extraction of protein names from fasta proteome file to help in building a database with fields comprising protein name and its amino acid sequence. The objective of this work was in developing a MATLAB software that could automatically extract protein name and amino acid sequence information from fasta proteome file and assign them to a new database that comprises fields such as protein name, amino acid sequence, number of amino acid residues, molecular weight of protein and nucleotide sequence of protein. Information on number of amino acid residues came from the use of the length built-in function in MATLAB analyzing the length of the amino acid sequence of a protein. The final two fields were provided by MATLAB built-in functions molweight and aa2nt, respectively. Molecular weight of proteins is useful for a variety of applications while nucleotide sequence is essential for gene synthesis applications in molecular cloning. Finally, the MATLAB software is also equipped with an error check function to help detect letters in the amino acid sequence that are not part of the family of 20 natural amino acids. Sequences with such letters would constitute as error inputs to molweight and aa2nt, and would not be processed. Collectively, given that important information such as protein name is enmeshed in a character array in fasta proteome file, this work sets out to develop a MATLAB software that could automatically extract protein name and amino acid sequence information, and assigns them to a new protein database. Using built-in functions, number of amino acid residues, molecular weight and nucleotide sequence of each protein were calculated; thereby, yielding a new protein database with improved functionalities that could support a variety of biology workflows ranging from sequence alignment to molecular cloning.

scholarly journals Glutamine as a precursor to N-terminal pyrrolid-2-one-5-carboxylic acid in mouse immunoglobulin λ-type light chains. Amino acid-sequence variability at the N-terminal extra piece of λ-type light-chain precursors

1977 ◽  
Vol 165 (2) ◽  
pp. 347-354 ◽  
Author(s):  
Yigal Burstein ◽  
Israel Schechter
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Sequence Data ◽  
Amino Acid Residues ◽  
Sequence Analyses ◽  
Methionine Residue ◽  
Mouse Immunoglobulin ◽  
V Region

The mRNA molecules coding for three mouse immunoglobulin λ-type light (L) chains (MOPC-104E λ1, RPC-20 λ1, MOPC-315 λ2) programme the cell-free synthesis of precursors larger than the mature proteins. Radioactive amino acid-sequence analyses of each of the three precursors labelled with [3H]alanine, [3H]serine, [3H]glutamine, [3H]glutamic acid and [3H]threonine showed that an extra piece, at least 18 residues long, is linked to the N-terminus of the mature L-chains. The N-terminal extra-peptide segment may be 19 residues long, since analyses of precursors labelled with [35S]methionine indicated an additional N-terminal methionine residue which was recovered in low yields. Presumably this is the initiator methionine, which is known to be short lived in eukaryotes. The mature forms of MOPC-104E, RPC-20 and MOPC-315 λ L-chains are blocked at the N-termini by pyrrolid-2-one-5-carboxylic acid (pyroglutamic acid). Sequence analyses of precursors labelled with [3H]glutamine and [3H]glutamic acid showed incorporation only of glutamine in a position that matches with the position of pyrrolid-2-one-5-carboxylic acid in the mature forms of all three precursors, and incorporation of glutamic acid in other positions. The data showed the absence of glutamine–glutamic acid interconversion, since the radioactive peaks obtained from either3H-labelled amino acid were discrete, and free from cross-contamination. These results prove that glutamine is the precursor amino acid of pyrrolid-2-one-5-carboxylic acid at the N-termini of the mature MOPC-104E λ1, RPC-20 λ1 and MOPC-315 λ2 L-chains. Thus the formation of pyrrolid-2-one-5-carboxylic acid by cyclization of glutamine is a post-translational event which occurs after, or concomitant with, cleavage of the extra piece from the precursor to yield the mature L-chain. The variable (V) regions (110 amino acid residues) of mouse λ L-chains are quite similar: when compared with that of MOPC-104E λ1 chain, the V-region of RPC-20 λ1 chain differs in one residue, and the V-region of MOPC-315 λ2 chain differs in 11 residues. The partial sequence data show that the N-terminal extra pieces of the two λ1 L-chain precursors have, so far, identical partial sequences; the extra piece of the λ2 L-chain precursor differs from these in at least three out of 19 positions.

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