Purification and characterization of trypsin from the poikilotherm <i>Gadus morhua</i>

Ágeirsson, Bjarni; Fox, Jay W.; Bjarnason, Jón B.

doi:10.1111/j.1432-1033.1989.tb14618.x

Cited by 174 publications

(164 citation statements)

References 48 publications

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“…Multiple numbers of these amino acids are frequently found within proteins that can explain the deactivation of a wide spectrum of viruses by ColdZyme. Trypsin from Atlantic cod (Gadus morhua) has been shown to have higher catalytic efficiency than comparable enzymes [11][12][13][14][15]. Furthermore, native proteins, such as those found on the surface of viruses, appear to be more readily hydrolyzed by cod trypsin [15].…”

Section: Discussionmentioning

confidence: 99%

A medical device forming a protective barrier that deactivates four major common cold viruses

Stefansson¹,

Guðmundsdóttir²,

Clarsund³

2017

Virol Res Rev

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The medical device ColdZyme is a mouth spray that forms a barrier in the throat against common cold viruses. The barrier solution of the device is composed of glycerol and Atlantic cod trypsin. The aim of this study was to evaluate the virus deactivating ability of ColdZyme against four major common cold viruses. A virucidal efficacy suspension test was conducted using ColdZyme against each of the challenge viruses in suspension. ColdZyme deactivated rhinovirus type 1A by 91.7% (1.08 log 10 ), rhinovirus type 42 by 92.8% (1.14 log 10 ), human influenza A virus H3N2 by 96.9% (1.51 log 10 ), respiratory syncytial virus (RSV) by 99.9% (2.94 log 10 ) and adenovirus type 2 by 64.5% (0.45 log 10 ). Based on the results, ColdZyme showed an effective broad-spectrum impact against common cold viruses. Thus, ColdZyme might represent a device with clinical benefits in prevention and treatment of respiratory viral infections by deactivating viruses within the respiratory tract.

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Section: Discussionmentioning

confidence: 99%

A medical device forming a protective barrier that deactivates four major common cold viruses

Stefansson¹,

Guðmundsdóttir²,

Clarsund³

2017

Virol Res Rev

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“…Trypsins from most marine organisms studied are anionic and in most cases more than one form is found (Asgeirsson et al, 1989). For trypsin from the North Atlantic salmon, for example, there are three forms with pl values of 5.3, 4.8 and 4.7, respectively (Arnesen, 1989).…”

Section: Introductionmentioning

confidence: 99%

“…Most of the fish trypsins have a temperature optimum similar to the mammalian enzymes, but several trypsins from marine sources are less stable at higher temperatures than their mammalian equivalents (Hjelmeland & Raa, 1982;Asgeirsson et al, The lower working temperature found for fish trypsins and the other properties unique for these fish enzymes as described above, are most likely related to the three-dimensional structure, and interests in gene modification of fish trypsins have recently been expressed (Nordisk Industrifond Protein Engineering Programme, Inaugural Symposium, September, 1989). We therefore initiated a structure study of trypsins from different fish species (Smalls, 1990;Smalhs, Hordvik, Hansen, Hough, Jynge, 1990), and the results from a 1.82 A X-ray crystallographic structure study of trypsin from the North Atlantic salmon (Salmo salar) as found in crystal form I (Smalls et al, 1990) are presented here.…”

Section: Introductionmentioning

confidence: 99%

“…However, trypsins from several cold-blooded species have been studied enzymatically, namely trypsin from shrimp (Walsh, 1970), starfish (Winter & Neurath, 1970), dogfish (Titani, Ericsson, Neurath & Walsh, 1975), sardine (Murakami & Noda, 1981), capelin (Hjelmeland & Raa, 1982), the Greenland cod (Simpson & Haard, 1984), the chum salmon (Uchida, Tsukayama & Nishide, 1984;Uchida, Anzai & Nishide, 1986), the Atlantic cod (Asgeirsson, Fox & Bjarnason, 1989), and the North Atlantic salmon (Arnesen, 1989;Torrissen, 1984).…”

Section: Introductionmentioning

confidence: 99%

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Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 Å resolution

Smalås

Hordvik²

1993

Acta Cryst D

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The structure of the serine protease trypsin from the North Atlantic salmon (Salmo salar) has been solved by molecular replacement and refined by restrained least-squares methods to a conventional R factor of 16.4% using diffractometer data in the 6.0-1.82 A resolution range (14443 reflections greater than 3tr). The model comprises 1793 protein atoms and 180 solvent molecules which were given unit occupancies, and the average temperature factors for protein atoms and solvent oxygen atoms are 15.2 and 36.8 A 2, respectively. The estimated error in atomic positions is about 0.2 A. The structure of salmon trypsin was solved and refined with only a small part of the amino-acid sequence known. However, a gene sequence of salmon trypsin has later become available. Some discrepancies between this sequence and the sequence obtained from the present X-ray crystal study indicate that the mentioned sequences may correspond to isoenzymes. The structure of salmon trypsin is similar to other trypsins of known structure.

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“…25) These trypsins display substantially higher catalytic efficiency than their mammalian counterparts. [25][26][27][28][29][30][31][32][33] We previously reported the chum salmon trypsin-catalyzed synthesis of peptides using inverse substrates. 23,24) We had obtained commercially available Atlantic cod trypsin at almost the same time.…”

mentioning

confidence: 99%

Atlantic Cod Trypsin-Catalyzed Peptide Synthesis with Inverse Substrates as Acyl Donor Components

Fuchise

Kishimura

Zhi-yong

et al. 2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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A large number of biologically active peptides have been isolated recently from bacterial, fungal, plant and animal sources and characterized in some detail. In particular, shortsequence peptides play important roles in the sensory appreciation of food toward four basic taste sensations (sweet, bitter, sour and salty). 1) Such peptides sometimes contain Damino acid and other unusual amino acids. Synthetic chemistry has witnessed remarkable progress with the development of novel biologically active peptides. Enzymatic peptide synthesis has emerged as a powerful approach to the preparation of short sequences. Especially, peptide synthesis using protease-catalyzed reverse reaction has been extensively studied with a variety of amino acids and peptide derivatives as coupling components. [2][3][4][5][6][7][8] It has been reported that the protease-catalyzed peptide synthesis is superior to the chemical coupling method because it is highly stereoselective, racemization-free, and requires less side-chain protection. The major drawback of the enzymatic method, however, is the respective substrate specificity. Thus, the application of proteases for peptide synthesis has not been fully investigated synthetic possiblity of a number of biologically significant peptides containing D-amino acid or other unusual amino acids. A few previous reports have shown the enzymatic condensation of noncorded amino acids, 9,10) peptide mimetics, 11) peptide conjugates, 12) and D-amino acid. 13) Previously, we reported that the inverse substrates such as p-amidino-14) and p-guanidinophenyl esters [15][16][17] behave as specific substrates for trypsin and trypsin-like enzymes and allow the specific introduction of an acyl group carrying a non-specific residue into the enzymatic active site. The characteristics of inverse substrates suggested that they are useful for enzymatic peptide synthesis. [18][19][20][21][22][23][24] Many studies on the characterization of trypsins from cold-adapted species have been reported. 25) These trypsins display substantially higher catalytic efficiency than their mammalian counterparts. [25][26][27][28][29][30][31][32][33] We previously reported the chum salmon trypsin-catalyzed synthesis of peptides using inverse substrates. 23,24) We had obtained commercially available Atlantic cod trypsin at almost the same time. We are interested in comparing of the catalytic efficiency of Atlantic cod trypsin with chum salmon trypsin. In the present work, we investigated Atlantic cod trypsin-catalyzed peptide synthesis using p-amidino-and p-guanidinophenyl esters of N atert-butyloxycarbonyl (Boc)-amino acid as acyl donor components with two types of acyl acceptors. We have found that Atlantic cod trypsin-catalyzed peptide synthesis of the Damino acid and b-amino acid-containing products is more efficient than chum salmon trypsin-catalyzed synthesis. Results and DiscussionThe kinetic constants for the trypsin-catalyzed hydrolysis of synthetic inverse substrates were analyzed on the basis of the following scheme.Where: Eϭe...

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Purification and characterization of trypsin from the poikilotherm Gadus morhua

Cited by 174 publications

References 48 publications

A medical device forming a protective barrier that deactivates four major common cold viruses

A medical device forming a protective barrier that deactivates four major common cold viruses

Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 Å resolution

Atlantic Cod Trypsin-Catalyzed Peptide Synthesis with Inverse Substrates as Acyl Donor Components

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