scholarly journals Type II intermediate-filament proteins from wool. The amino acid sequence of component 5 and comparison with component 7c

1992 ◽  
Vol 282 (1) ◽  
pp. 291-297 ◽  
Author(s):  
L G Sparrow ◽  
C P Robinson ◽  
J Caine ◽  
D T W McMahon ◽  
P M Strike
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intermediate Filament ◽  
Sequence Similarity ◽  
British Library ◽  
Intermediate Filament Protein ◽  
Type Ii ◽  
Blocking Group ◽  
Intermediate Filament Proteins ◽  
Merino Wool

Component 5 is one of the four type II intermediate-filament proteins found in the hard keratin wool. It was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage. Component 5 is an N-terminally blocked molecule of 503 residues and Mr (not including the blocking group) of 56,600. The blocking group has not been identified. The amino acid sequence of component 5 shows 77% sequence identity with that of component 7c, another type II wool intermediate-filament protein [Sparrow, Robinson, McMahon & Rubira (1989) Biochem. J. 261, 1015-1022]. The sequence similarity extends from the N-termini of the two molecules to residue 459 (component 5 sequence); however, there is no recognizable sequence similarity in the remaining C-terminal 43 amino acid residues. Details of procedures used in determining the sequence of component 5 have been deposited as a Supplementary Publication SUP 50168 (80 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire, LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1992) 281, 5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 5, peptide CN1, the peptide mixture CN2/3 and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, and (3) details of the method used to determine the C-terminal sequence of component 5.

scholarly journals The amino acid sequence of component 7c, a type II intermediate-filament protein from wool

1989 ◽  
Vol 261 (3) ◽  
pp. 1015-1022 ◽  
Author(s):  
L G Sparrow ◽  
C P Robinson ◽  
D T W McMahon ◽  
M R Rubira
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
British Library ◽  
Intermediate Filament Protein ◽  
Type I ◽  
Type Ii ◽  
Blocking Group ◽  
Intermediate Filament Proteins

Component 7c is one of the four homologous type II intermediate-filament proteins that, by association with the complementary type I proteins, form the microfibrils or intermediate filaments in wool. Component 7c was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage reactions. It is an N-terminally blocked molecule of 491 residues and Mr (not including the blocking group) of 55,600; the nature of the blocking group has not been determined. The predicted secondary structure shows that component 7c conforms to the now accepted pattern for intermediate-filament proteins in having a central rod-like region of approximately 310 residues of coiled-coil alpha-helix flanked by non-helical N-and C-terminal regions. The central region is divided by three non-coiled-coil linking segments into four helical segments 1A, 1B, 2A and 2B. The N-and C-terminal non-helical segments are 109 and 71 residues respectively and are rich in cysteine. Details of procedures use in determining the sequence of component 7c have been deposited as a Supplementary Publication SUP 50152 (65 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257,5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 7c, peptides CN1, CN2 and CN3, and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, (3) details of methods used to determine the C-terminal sequence of peptide CN3, and (4) detailed evidence to justify a number of corrections to the previously published sequence.

scholarly journals The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis

1987 ◽  
Vol 246 (1) ◽  
pp. 115-120 ◽  
Author(s):  
R P Ambler ◽  
T E Meyer ◽  
M A Cusanovich ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
British Library ◽  
Sequence Information ◽  
Cytochrome C2 ◽  
Percentage Sequence Identity ◽  
Acidophilic Bacterium ◽  
High Degree ◽  
Rhodopseudomonas Globiformis

The amino acid sequence of the principal soluble cytochrome c from the phototrophic acidophilic bacterium Rhodopseudomonas (or Rhodopila) globiformis was determined. By the criteria of percentage sequence identity and fewness of internal insertions and deletions it is more similar in sequence to some mitochondrial cytochromes c than to any known bacterial cytochrome. The organism does not have any properties that commend it as being particularly similar to postulated prokaryotic precursors of the mitochondrion. We consider that the relatively high degree of sequence similarity is an instance of convergence, and is an example of the limitations that are imposed on attempts to deduce distant evolutionary relationships from sequence information. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50136 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

scholarly journals The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae)

1991 ◽  
Vol 277 (2) ◽  
pp. 335-340 ◽  
Author(s):  
V B Cronin ◽  
B Maras ◽  
D Barra ◽  
S Doonan
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Aspartate Aminotransferase ◽  
Baker’S Yeast ◽  
High Yield ◽  
British Library ◽  
Baker's Yeast ◽  
Yeast Saccharomyces Cerevisiae ◽  
Blocking Group

1. The single (cytosolic) aspartate aminotransferase was purified in high yield from baker's yeast (Saccharomyces cerevisiae). 2. Amino-acid-sequence analysis was carried out by digestion of the protein with trypsin and with CNBr; some of the peptides produced were further subdigested with Staphylococcus aureus V8 proteinase or with pepsin. Peptides were sequenced by the dansyl-Edman method and/or by automated gas-phase methods. The amino acid sequence obtained was complete except for a probable gap of two residues as indicated by comparison with the structures of counterpart proteins in other species. 3. The N-terminus of the enzyme is blocked. Fast-atom-bombardment m.s. was used to identify the blocking group as an acetyl one. 4. Alignment of the sequence of the enzyme with those of vertebrate cytosolic and mitochondrial aspartate aminotransferases and with the enzyme from Escherichia coli showed that about 25% of residues are conserved between these distantly related forms. 5. Experimental details and confirmatory data for the results presented here are given in a Supplementary Publication (SUP 50164, 25 pages) that has been deposited at the British Library Document Supply Centre, Boston Spa. Wetherby, West Yorkshire LS23 7 BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1991) 273, 5.

scholarly journals The amino acid sequence of rabbit slow-muscle troponin I.

1977 ◽  
Vol 167 (1) ◽  
pp. 183-192 ◽  
Author(s):  
Roger J. A. Grand ◽  
J. Michael Wilkinson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Troponin I ◽  
Proteolytic Enzymes ◽  
Vastus Lateralis ◽  
Slow Muscle ◽  
British Library ◽  
Blocking Group ◽  
Single Polypeptide Chain ◽  
N Terminus

Troponin I was isolated from six red muscles in the hind leg of the rabbit. Soleus, semi-tendinosus, vastus intermedius and adductor longus muscles contained primarily slow-muscle troponin I, vastus lateralis contained fast-muscle troponin I and quadratus femoris contained a mixture of the two. The complete amino acid sequence of the troponin I from slow muscle was determined. Seven CNBr fragments were isolated and sequenced by using the dansyl–Edman technique after digestion with proteolytic enzymes. The CNBr fragments were ordered by isolation of tryptic peptides containing carboxy[14C]methyl-methionine. Direct evidence for the conjunction of residues 8 and 9 has not been obtained, and one of the carboxyl groups between residues 71 and 79 may carry an amide group. Slow-muscle troponin I is a single polypeptide chain of 184 residues with a mol.wt. of 21146. It has a net overall positive charge of 18 at pH7, and an absorption coefficient, A1%,1cm280, of 5.43. The protein was isolated with both a blocked and an unblocked N-terminus, although the nature of the blocking group was not determined. Proline was found to be the N-terminal amino acid. Two forms of the protein could also be distinguished by the presence of an extra two residues at the C-terminus. Comparison of sequences of troponin I from rabbit slow, fast and cardiac muscle shows that homology is most marked in the C-terminal half of the molecules. Towards the N-terminus the homology becomes much less marked. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50079 (32 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained in the terms given in Biochem. J. (1977), 161, 1.

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