Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The complete amino acid sequence of the major component myoglobin from the Pacific spotted dolphin, Stenella attenuata graffmani, was determined by the automated Edman degradation of several large peptides obtained by specific cleavage of the protein. The acetimidated apomyoglobin was selectively cleaved at its two methionyl residues with cyanogen bromide and at its three arginyl residues by trypsin. By subjecting four of these peptides and the apomyoglobin to automated Edman degradation, over 80% of the primary structure of the protein was obtained. The remainder of the covalent structure was determined by the sequence analysis of peptides that resulted from further digestion of the central cyanogen bromide fragment. This fragment was cleaved at its glutamyl residues with staphylococcal protease and its lysyl residues with trypsin. The action of trypsin was restricted to the lysyl residues by chemical modification of the single arginyl residue of the fragment with 1,2-cyclohexanedione. The primary structure of this myoglobin proved to be identical with that from the Atlantic bottlenosed dolphin and Pacific common dolphin but differs from the myoglobins of the killer whale and pilot whale at two positions. The above sequence identities and differences reflect the close taxonomic relationship of these five species of Cetacea.
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PMID:Complete amino acid sequence of the myoglobin from the Pacific spotted dolphin, Stenella attenuata graffmani. 45 57

The complete amino acid sequence of the major component myoglobin from Pacific sei whale, Balaenoptera borealis, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. The acetimidated apomyoglobin was selectively cleaved at its two methionyl residues with cyanogen bromide and at its three arginyl residues by trypsin. From the sequence analysis of four of these peptides and the apomyoglobin, over 75% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by the sequence analysis of peptides that resulted from further digestion of the amino-terminal and central cyanogen bromide fragments. The amino-terminal fragment was specifically cleaved at its two tryptophanyl residues with N-chlorosuccinimide and the central cyanogen bromide fragment was cleaved at its glutamyl residues with staphylococcal protease and at its single tyrosyl residue with N-bromosuccinimide. The primary structure of this myoglobin proved identical with that from the gray whale but differs from that of the finback whale at four positions, from that of the minke whale at three positions and from the myoglobin of the humpback whale at one position. The above sequence identities and differences reflect the close taxonomic relationship of these five species of Cetacea.
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PMID:Complete amino acid sequence of the myoglobin from the Pacific sei whale, Balaenoptera borealis. 45 58

The binding isotherms of native bovine serum albumin with cationic detergents, such as octyl, decyl, dodecyl and tetradecylpyridinium bromides were determined at pH 6.8 and 3.4 at 25 degrees C. The isotherms for dodecyl and tetradecylpyridinium bromides were also determined at 3 degrees C. The average number of detergent cations bound increased with increasing hydrocarbon chain length. At low detergent concentration the binding of all alkylpyridinium bromides was smaller at pH 3.4 than at pH 6.8. Dodecylpyridinium bromide was bound to native beta-lactoglobulin, aldolase, ovalbumin, haemoglobin, myoglobin, lysozyme, trypsin and ribonuclease at pH 6.8. No binding occurred to alpha-chymotrypsin and chymotrypsinogen. The free enthalpy change, --delta G degrees, calculated from intrinsic association constants K was determined.
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PMID:Protein-cationic detergent interaction. Equilibrium dialysis study of the interaction of bovine serum albumin and other proteins with alkylpyridinium bromide. 49 43

Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.
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PMID:Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide. 49 44

The amino acid sequence of the beta-chain of the principal haemoglobin from the shark H. portusjacksoni has been determined. The chain has 141 residues, the same as that of mammalian alpha-chains and less than the 146 residues of mammalian beta-chains or the 148 residues of the alpha-chain from the tetrameric shark haemoglobin. The sequence was deduced from the sequences of peptides obtained by digestion of the globin or its cyanogen bromide fragments with trypsin, chymotrypsin, pepsin and papain. The difference in length of the beta-chain is most readily accounted for by the absence of the D helix. This small helical section is normally present in myoglobins and beta-globins but absent in alpha-chains. The deduction that it is absent from shark beta-chain is based on consideration of homology. The beta-chain shows the insertion of histidine beta2 and the deletions corresponding to residues A17 and AB1 relative to alpha-and myoglobin chains. The reactive thiol group in shark haemoglobin was shown by radioactive labelling to be residue 51 in the beta-chain, immediately preceding the E helix. The amino acid sequence of shark beta-chain shows 92 differences from human beta-chain, significantly more differences than shown by chicken or frog beta-chains, in line with its earlier time of divergence. If the tertiary structure of the shark beta-chain is the same as that of the horse then there are two changes in the alpha1beta2 contact site in oxyhaemoglobin and an additional one in deoxyhaemoglobin. When both alpha- and beta-chain contacts are considered there is a total of nine changes in residues involved in the alpha1beta2 contacts. There is no Bohr effect in shark haemoglobin, and of the residues normally involved in this effect the C-terminal histidine residue of the beta-chain is present, but the aspartyl (FG1) residue to which it is salt-linked is not, being replaced by a glutamyl residue.
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PMID:Haemoglobins of the shark, Heterodontus portusjacksoni. III. Amino acid sequence of the beta-chain. 61 4

The complete amino acid sequence of the major component myoglobin from the pilot whale, Globicephala melaena, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. The apomyoglobin was selectively cleaved at the two methionyl residues with cyanogen bromide and the acetimidated apomyoglobin was cleaved at the three arginyl residues by trypsin. From the sequence analysis of four of these peptides and the apoprotein, over 90% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by sequence analysis of three of the tryptic peptides isolated from the central cyanogen bromide fragment after modification of its single arginyl residue with 1,2-cyclohexanedione. This myoglobin differs from that of the Black Sea dolphin at four positions and from the myoglobin of the killer whale, Pacific common dolphin, and Atlantic bottlenosed dolphin at two positions. The above differences reflect the close taxonomic relationship of these five species of Cetacea. This sequence determination was aided by the use of a Texas Instruments 980A minicomputer system which performed peak integrations for all samples subjected to amino acid analysis.
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PMID:Complete amino acid sequence of myoglobin from the pilot whale, Globicephala melaena. 65 76

The C-terminal cyanogen bromide fragment of myoglobin from bottle nosed dolphin was digested with trypsin and two different derivatives of the digest were prepared, one being deuteroacetylated and deuteropermethylated, the other being submitted to one step of Edman degradation and then acetylated and permethylated. Comparison of the results obtained by computerized interpretation of the mass spectra of these two derivatives, combined with previous information about the sample, facilitated the sequence determination of all the peptides in the sample. Alignment of the peptides could then be carried out by homology with myoglobin from other cetaceans.
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PMID:Determination of the amino acid sequence of the C-terminal cyanogen bromide fragment of myoglobin from bottle nosed dolphin by mass spectrometric peptide mixture analysis. 65 60

Native human oxyhemoglobin, which has a rigid conformation resistant to proteases such as trypsin and subtilisin, could be hydrolyzed by these proteases at pH 7.0 after treatment with p-chloromercuribenzoate. The digestion curve of hemoglobin as a function of concentration of the mercurial was essentially parallel to the titration curve of hemoglobin with the mercurial, indicating that a relationship exists between susceptibility to proteases and modification of thiol groups of the protein. On the other hand, when myoglobin was used as a substrate, the degree of proteolysis did not increase after treatment with the mercurial. Circular dichroism measurements and gel-filtration experiments showed that the observed increase in susceptibility of hemoglobin to proteases was not due to a conformational change involving unfolding of alpha-helical structure, but was due to the dissociation of the tetrameric hemoglobin molecule into dimer and monomer after treatment with the mercurial.
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PMID:Increase in the susceptibility of hemoglobin to proteases upon treatment with p-mercuribenzoate. 69 99

The complete primary structure of the major component myoglobin from the humpback whale, Megaptera novaeangliae, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Over 80% of the amino acid sequence was established from the three peptides resulting from the cleavage of the acetimidated apomyoglobin at the three arginine residues with trypsin. The further digestion of the central cyanogen bromide peptide with trypsin and S. aureus strain V8 protease enabled the determination of the remainder of the covalent structure. This myoglobin differs from that of sperm whale, Physeter catodon, at 12 positions, and dwarf sperm whale, Kogia simus, at 14 positions, finback whale Balaenoptera physalus at 3 positions, minke whale, Balaenoptera acutorostrata at 2 positions, and California gray whal Eschrichtius gibbosus, at 1 position. All of the substitutions observed in this sequence fit readily into the three-dimensional structure of sperm whale myoglobin.
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PMID:Complete amino acid sequence of the major component myoglobin from the humpback whale, Megaptera novaeangliae. 69 93

The complete primary structure of the major component myoglobin from the Arctic minke whale, Balaenoptera acutorostrata, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Over 80% of the amino acid sequence was established from the three peptides resulting from the cleavage of the apomyoglobin at the two methionine residues with cyanogen bromide along with the four peptides resulting from the cleavage of the methylacetimidated apomyoglobin at the three arginine residues with trypsin. The further digestion of the central cyanogen bromide peptide with trypsin and S. aureus strain V8 protease enabled the determining of the remainder of the covalent structure. This myoglobin differs from that of the dwarf sperm whale, Kogia simus, at 16 positions, and the common dolphin, Delphinus delphis, at 14 positions, from that of the common porpoise, Phocaena phocaena, and the bottlenosed dolphin, Tursiops truncatus at 13 positions, from that of the Amazon River dolphin, Inia geoffrensis, at 10 positions, and from that of California gray whale, Eschrichtius gibbosus, at 3 positions- All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm whale myoglobin.
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PMID:The complete amino acid sequence of the major component myoglobin from the arctic minke whale, Balaenoptera acutorostrata. 83 10


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