Stability of serine collagenolytic protease a from hepatopancreas of crab Paralithodes camtschatica

Sakharov, Ivan Yu.; Litvin, F. E.

doi:10.1016/0305-0491(90)90136-h

Cited by 7 publications

(3 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One of them, which catalyzes the degradation of collagen, is reversibly inactivated with the metal chelating agents 1,lO phenanthroline and EDTA. However, some preparations of collagenolytic enzymes from crab hepatopancreas also have activities resembling those of the serine class proteinases (Sakharov and Litvin 1990). The presence of an enzyme with collagenase activity in 4P and CRF is suggested by the present data and by those found in krill proteinases (Osnes 1985), crab (Sakharov and Litvin 1990) and crayfish (Stocker et al 1988;Sova el al.…”

Section: Discussionsupporting

confidence: 62%

Characterization of Proteinase Classes in Langostilla (Pleuroncodes Planipes) and Crayfish (Pacifastacus Astacus) Extracts

García‐Carreño¹,

Haard

1993

J Food Biochemistry

206

View full text Add to dashboard Cite

Proteinases (EC 3.4.21‐24) in langostilla extract and crayfish hepatopancreas were classified using site specific effectors or chelators for either serine, cysteine, aspartic or metallo classes. Azocasein hydrolysis by langostilla and crayfish preparations was inhibited 50% and 40%, respectively, when assayed in the presence of serine proteinase inhibitor, phenylmethylsulfonyl fluoride. A similar degree of inhibition was observed with a trypsin inhibitor. However, no inhibition occurred with a chymotrypsin inhibitor. Less inhibition of azocasein hydrolysis, i.e., 20% and 14%, respectively, resulted with 1,10 phenanthroline. Inhibitors for cysteine and aspartic proteinases did not reduce the azocasein hydrolysis activities significantly. The amidase activity, with N‐benzoyl‐DL‐Arg‐p‐nitroanilide as substrate was more sensitive, in both extracts, to serine proteinase inhibitors than the azocasein hydrolase activity. Results showed the presence of serine proteinases, i.e., trypsin but not chymotrypsin, as the major component and some minor activity of metallo dependent proteinases in the decapods extracts. Zymograms obtained after SDS‐PAGE showed a dozen proteinases in each extract. Some of them were inhibited by a serine proteinase inhibitor and two to three were inhibited by 1,10 phenanthroline, supporting the results of the test tube proteinase activity assays. Furthermore, the reported technique for zymograms allowed direct comparison between extracts and provided information about their composition and the molecular weight of the targeted enzymes.

show abstract

Section: Discussionsupporting

confidence: 62%

Characterization of Proteinase Classes in Langostilla (Pleuroncodes Planipes) and Crayfish (Pacifastacus Astacus) Extracts

García‐Carreño¹,

Haard

1993

J Food Biochemistry

206

View full text Add to dashboard Cite

show abstract

“…The molecular weights of previously characterized digestive collagenases are similar to that of chymotrypsin, ranging from 25 to 27 kDa (Sakharov et al, 1988;Eisen etal., 1973). All of the active zones in the molecular weight range of 20-30 kDA were partially inhibited by the serine protease inhibitor PMSF (Garda-Carrefio and Haard, 1993).…”

Section: Resultsmentioning

confidence: 97%

Enzymes with Peptidase and Proteinase Activity from the Digestive Systems of a Freshwater and a Marine Decapod

García‐Carreño¹,

Hernández-Cortés²,

Haard³

1994

J. Agric. Food Chem.

108

View full text Add to dashboard Cite

“…Collagenolytic protease cotnposed of two isozytnes and elastase appeared to underly this proteolytic activity (1)(2)(3). Using ion-exchange chromatography, these proteases were purified to a homogeneity, which enabled us to study their molecular and catalytic properties (2)(3)(4)(5)(6).…”

mentioning

confidence: 99%

Immunohistochemical study of purulent wounds treated with King crab collagenase

Sakharov

Shekhonin

Glyanzev

et al. 1994

Experimental Dermatology

View full text Add to dashboard Cite

Immunohistochemical study of tissues from purulent wounds in rats after treatment with the collagenase isolated from the King crab Paralithodes camtschatica was undertaken. The enzymotherapy resulted in a rapid and efficient removal of necrotic debris. It was accompanied by fibrin elimination from the wound bed and subsequent formation of new capillaries. Cellular fibronectin with ED-A sequence was identified in the newly formed granulation tissue, which points to its active synthesis in situ. Polyclonal antibodies against two isozymes of the crab collagenolytic protease were obtained. By their use it was shown that, after application of the collagenase, both isozymes accumulated in fibrin deposits at the wound bed but did not penetrate adherent granulation tissue.

show abstract

Stability of serine collagenolytic protease a from hepatopancreas of crab Paralithodes camtschatica

Cited by 7 publications

References 11 publications

Characterization of Proteinase Classes in Langostilla (Pleuroncodes Planipes) and Crayfish (Pacifastacus Astacus) Extracts

Characterization of Proteinase Classes in Langostilla (Pleuroncodes Planipes) and Crayfish (Pacifastacus Astacus) Extracts

Enzymes with Peptidase and Proteinase Activity from the Digestive Systems of a Freshwater and a Marine Decapod

Immunohistochemical study of purulent wounds treated with King crab collagenase

Contact Info

Product

Resources

About