Purification and characterization of acid cysteine proteinase from squid mantle muscle

Sakai-Suzuki, Junko; Tobe, Masahiro; Tsuchiya, Takahide; Matsumoto, Juichiro J.

doi:10.1016/0305-0491(86)90192-6

Cited by 7 publications

(3 citation statements)

References 13 publications

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“…Finally, it was proved that metallo-, cystein-, and serine-proteinases were the three major enzymes. The conclusion was the confirmation of the previous results appeared in the separate papers [4][5][6][7][8][9][10][11]. Among the three, metallo-type was the most active at neutral pH with native myofibrils.…”

Section: Discussionsupporting

confidence: 79%

“…One of the successful applications of the high activity of these enzymes was a rapid fermentation of fish sauce [3]. Proteinases found in squid liver are metallo-proteinase [4][5][6][7], cystine-proteinase [8][9][10], serine-proteinase [11] and cathepsin D-like cystein-proteinase [12]. The information on the properties of proteinases in squid liver was accumulated, but many papers handled a single enzyme contained in the organ and there is little information on the contribution of respective enzymes in the activity of whole enzymes contained in liver.…”

Section: Introductionmentioning

confidence: 99%

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Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

et al. 2010

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Three types of proteinases, namely cystein-, metallo-, and serine-proteinases were found in squid hepatopancreas by studying the inhibition spectra using carp myofibril as substrates. Cystein-, metallo-, and serine-type showed the highest activities at 50 ºC, 35 ºC, and 40 ºC, respectively. The optimal pHs were pH 5, pH 7, and pH 9 for cystein-, metallo-, and serine-type, respectively. When assayed at 20 ºC and pH7.5, metallo-type showed the highest activity. Metallo-type was characterized by a high selectivity in the digestion of myosin. Among the three enzymes, cystein-type was found to be the most stable against thermal and acid treatments. Heat treated myofibrils were more susceptible to cystein-and serine-types, but less susceptible to metallo-type. Acid treatment of myofibrils also enhanced the digestibility by cystein-type. The results indicated that cystein-type seemed to be the most suitable enzyme to produce peptides from denatured myofibrils by their random digestion.

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Section: Discussionsupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

et al. 2010

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“…Leupeptin-TOYOPEARL gel was prepared according to the method of Sakai-Suzuki et al [17]. First, 20 ml of the crude extract was diluted with a similar volume of water and applied to 2 ml of the leupeptin-TOYOPEARL gel equilibrated with buffer II (50 mM phosphate buffer (pH 6.0), containing 0.05 mM EDTA and 0.01% NaN 3 ), after which it was circulated at a flow rate of 0.5 ml/min overnight.…”

Section: Purification Of a Squid Cysteine Proteasementioning

confidence: 99%

A Cysteine-Activated Protease Isolated fromTodarodesPacificusSquid Degrades Collagen Below its Denaturation Temperature

Miura-Yokota¹,

Matsubara²,

Ebihara³

et al. 2004

Connective Tissue Research

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Collagen purified from the mantle muscle of the Japanese common squid, Todarodes pacificus, showed autodegradation during incubation under acidic conditions at 25 degrees C, without the addition of exogenous enzymes. This suggests that the collagenolytic proteases bind to collagen tightly through the steps of collagen preparation. Collagenolytic activity also was detected in a crude extract of mantle muscle, and leupeptin and E-64 were observed to inhibit collagenolytic activity within the collagen fraction and muscle extract. We purified these collagenolytic cysteine proteases by leupeptin column chromatography and cellulose acetate membrane electrophoresis. Optimal enzymatic activity was observed at pH 3.5, and collagenolytic activity was completely suppressed at neutral or alkaline pH. The purified enzymes were 28 kDa and 25 kDa in size, and both had gelatinolytic activity, as detected by gelatin zymography, and cut the specific site of denatured collagen alpha chain. The purified enzymes degraded squid collagen at 25 degrees C, which is 2.5 degrees lower than the temperature at which squid collagen normally denatures; however, the proteases were ineffective at 20 degrees C. Interestingly, the isolated proteases were capable of digesting both squid and bovine gelatin. In this article, we describe collagenolytic cysteine proteases that bind to the collagen of Todarodes pacificus, thereby digesting it by attacking microunfolding regions generated by incubation 2-3 degrees C below the denaturation temperature.

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Cloning and nucleotide sequence of a novel 28-kDa protein from the mantle muscle of the squid Todarodes pacificus with homology to tropomyosin

Miura-Yokota

Matsubara

Ebihara

et al. 2005

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Purification and characterization of acid cysteine proteinase from squid mantle muscle

Cited by 7 publications

References 13 publications

Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

A Cysteine-Activated Protease Isolated fromTodarodesPacificusSquid Degrades Collagen Below its Denaturation Temperature

Cloning and nucleotide sequence of a novel 28-kDa protein from the mantle muscle of the squid Todarodes pacificus with homology to tropomyosin

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