The action of proteinase A2 of Actinidia chinensis on the B-chain of oxidized insulin

McDowall, Max A.

doi:10.1016/0005-2744(73)90395-1

Cited by 20 publications

(9 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lane G shows the action of papain at 18 U/mL on the myosin HC extract of Lane E. All the myosin was degraded with the production of low molecular weight products from 17,000 D to 14,000 D. It is interesting to note that the two bands in the myosin extract (lane E) with apparent molecular weights of 20,700 D and 16,600 D were not hydrolyzed by papain. Lane H shows two bands of actinidin (bands 7 and 8) A, and A,, respectively, as also found by McDowall (1973).…”

Section: Lanesupporting

confidence: 72%

“…Carne and Moore (1978) determined the molecular weight to be 23,500 by amino acid sequence of the enzyme. McDowall (1973) fractionated actinidin, extracted in its active form, on DEAE-Sephadex A25 (pH 5.0) and found two active components, each homogeneous on PAGE and designated them as A, and A, in order of increasing electrophoretic mobility towards the anode.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Application of Actinidin From Kiwifruit to Meat Tenderization and Characterization of Beef Muscle Protein Hydrolysis

Lewis

Luh

1988

J Food Biochemistry

View full text Add to dashboard Cite

The effect of actinidin on the I'enderness of broiled bovine semitendinosus (ST) steaks was studied, An actinidin activity of 400 U/mL resulted in Kramer shear values and sensory tenderness scores equivalent to that produced by Adolph's papain-based meat tenderizer (18 U/rnL). Both were significantly (Pc0.05) more tender than steaks having no tenderizing treatment. Actinidin did not over-tenderize the steak surface as did Adolph5 meat tenderizer. Hydrolysis of myojibrillarproteins in enzyme-treated steaks prior to broiling was considerably less for actinidin than for papain when using activities to attain equal Kramer shear values of broiled steaks.Joiirnal i$Food Binthemistry 12 (1988) 147-15'8. All Rights Re.srried. 0 Copyright 1988 hy F00d & Nutrition P r m , I m : , Trumbulf, Connecticut. 147 148 DEBORAH A. LEWIS AND B.S. LUH Crude extracts of actinidin split 20% of the peptide bonds in a 3% gelatin gel in 15 min (1 mM cysteine, pH 4.3,0.25 M EDTA) and is more active toward hemoglobin

show abstract

Section: Lanesupporting

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Application of Actinidin From Kiwifruit to Meat Tenderization and Characterization of Beef Muscle Protein Hydrolysis

Lewis

Luh

1988

J Food Biochemistry

View full text Add to dashboard Cite

show abstract

“…3 and [7,8]). The same phenomenon is exhibited by ficin 171 and by Chinese gooseberry proteinase, as is apparent on comparison of the reported molecular weights [9,10]. Using the graphical procedure depicted in Fig.…”

Section: Methodssupporting

confidence: 69%

Dimerization of Papain Induced by Mercuric Chloride and a Bifunctional Organic Mercurial

Sluyterman

Wijdenes

Voorn

1977

European Journal of Biochemistry

View full text Add to dashboard Cite

The bifunctional mercurial meso-l,4-bis(acetatomercuri)-2,3-diethoxybutane and mercuric chloride are capable of dimerizing papain, by the attachment of the thiol group of two molecules of papain to each molecule of reagent. This is evident from the titration data, gel filtration and sedimentation equilibrium.The conformational change of papain necessary for this reaction is discussed.It has been shown recently [l] that one proton is released if one zinc ion or one methylmercuric ion is attached to the single essential thiol group of one papain molecule at pH 6. As will be reported in this paper, these experiments were repeated with mercuric chloride, a divalent metal which binds very strongly to thiol groups. The proton release proved to be different, in that two protons are released from two papain molecules on addition of one mercuric ion. It will be shown that this effect is due to the formation of a papain dimer. EXPERIMENTAL PROCEDUREActive papain, free from activators, was prepared in the following manner. A solution of 1 % mercuric papain, purified on the agarose-mercurial column [2], containing 10 mM phosphate, 20 mM dithiothreitol and 1 mM tetraethylenepentamine (Merck), pH 7.5, was stored for 10 min and concentrated to 10% of its initial volume, under nitrogen pressure, in a 'Diaflo' cell provided with a type-PM10 membrane (Aminco Corp.). The solution was readjusted to about the initial volume by addition of oxygen-free water containing 0.5 mM tetraethylenepentamine and 10 mM acetate pH 5.5 and concentrated again to 10% of the initial volume. Finally water was added containing 30 mM KCI and 0.1 mM acetate pH 5.5 and dialysis was carried out with the same solution in the 'Diaflo' Note. A preliminary report was presented at the 10th Meeting of the Federation of European Biochemical Societies, Paris, July 1975.Abbreviations. Reagent I, meso-l,4-bis(acetatomercuri)-2,3-diethoxybutane ; ClHgBzSO3, p-chloromercuribenzene sulphonate.Enzyme. Papain (EC 3.4.22.2).cell. The emerging solution was checked for thiol compounds by adding 1 ml of 10 mM 5,5'-dithio-bis(2-nitrobenzoic acid) in 0.1 M phosphate pH 8.0 to 3 ml eluent and measuring the absorbance at 440 nm [ 3 ] .When the absorbance was < 0.05, corresponding to a thiol concentration in the eluent of < 8 pM, the papain solution was subjected to one more cycle of tenfold dilution with the KCl/acetate buffer and reconcentration. The final solution contained 1-2% (0.4-0.8 mM) papain. Titrations were carried out in a quartz vessel. The pH was read on a Philips digital pH meter. The calomel electrode was separated from the vessel by an agarose-containing salt bridge. The solution was gently stirred with a magnetic stirrer. The mercurials were added in increments of 0.1 -1 .O ml. All solutions were made in distilled deionized water and deaerated in vacuo. The organic mercurials were p-chloromercuribenzene monosodium sulphonate (ClHgBzS03) purchased from Sigma Chem. Corp. (St Louis) and meso-1,4-bis(acetatomercuri)-2,3-diethoxybutane (reagent I) provided by Dr J. ...

show abstract

“…The concentration of actinidain was calculated from the absorbance at 280 nm by using the absorption coefficient, E (1.0 mg/ml) = 2.121. 30) The enzyme was inactivated by masking with S-methyl methanethiolsulfonate (Sigma-Aldrich, MO, USA) and kept at 5 C until its use.…”

Section: Methodsmentioning

confidence: 99%

Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (Thunnus albacares)

Morimoto

Kunii

Hamano

et al. 2004

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

The action of proteinase A2 of Actinidia chinensis on the B-chain of oxidized insulin

Cited by 20 publications

References 9 publications

Application of Actinidin From Kiwifruit to Meat Tenderization and Characterization of Beef Muscle Protein Hydrolysis

Application of Actinidin From Kiwifruit to Meat Tenderization and Characterization of Beef Muscle Protein Hydrolysis

Dimerization of Papain Induced by Mercuric Chloride and a Bifunctional Organic Mercurial

Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (Thunnus albacares)

Contact Info

Product

Resources

About