Sulphydryl-Disulphide Relationships in the Induction of Gels in Proteins by Urea

Huggins, Charles; Tapley, Donald F.; Jensen, Elwood V.

doi:10.1038/167592a0

Cited by 208 publications

(67 citation statements)

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“…These interactions of meat proteins may consist of disulfide linkages (Huggins et al, 1951), multiple hydrogen bonds (Eldridge and Ferry, 1954), peptide bonds (Bello, 1965), electrostatic and hydrophobic interactions (Wolf and Tamura, 1969).…”

Section: Massagingmentioning

confidence: 99%

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Reddy¹,

Mandal²,

Sen³

et al. 2014

International J. of Meat Science

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To provide the consumer with a highly palatable product at a reasonable cost is the main objective of any food industry. Particular to meat industry, utilization of less valuable carcasses and carcass cuts and carcass components (plates, flanks, shanks, etc.) is of prime interest in periods of economic pressure. One such relevantly new technological approach is restructuring technology, which enables the production of value-added meat products from low value cuts and trimmings of carcasses. Although the economics and processing of restructuring meats appear favourable to producing a product that has the palatability attributes that are between an intact muscle steak and ground meat. This review of restructured meat products discuss the actual science and technology behind the restructuring of muscles, how muscle chunks are binding each together at protein molecules stage, factors influencing the meat pieces binding, type of restructuring methodologies, quality attributes of restructured meat products, problems of oxidation, use of natural antioxidants and recommends research needs for the future.

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Section: Massagingmentioning

confidence: 99%

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Reddy¹,

Mandal²,

Sen³

et al. 2014

International J. of Meat Science

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“…Changes in S-S bond position could cause conformational variation in the 22K protein and account for the detection of 22Ka and 22Kb after denaturation in non-reducing SDS-PAGE. Shifts in S-S bond position in proteins dissolved in SDS or urea have previously been reported (Huggins et al, 1951;Cebra, t964;Gerber, 1964) and the sulphydryl-disulphide interchange reaction involved requires the presence of sulphydryl groups. The reaction may be prevented using the alkylating agent iodoacetamide which binds irreversibly to sulphydryl groups, preventing their participation in the interchange (Friedman, 1973).…”

mentioning

confidence: 99%

Heterogeneity of the Respiratory Syncytial Virus 22K Protein Revealed by Western Blotting with Monoclonal Antibodies

Routledge¹,

Willcocks

Morgan³

et al. 1987

Journal of General Virology

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SUMMARYRespiratory syncytial (RS) virus-infected HeLa, HEp-2, Veto and BS-C-1 cell lysates were electrophoresed on SDS-polyacrylamide gels under reducing conditions and analysed by Western blotting and immunoperoxidase using monoclonal antibodies specific for the 22K protein (relative tool. wt. of 23000 in our gel system). Three novel polypeptides with mol. wt. of 24000, 21000 and 17000 were stained in addition to the 23 000 polypeptide which was present in the greatest amount in all three virus strains tested regardless of host cell line. When samples were electrophoresed under nonreducing conditions each of the three higher mol. wt. polypeptides seen in reducing gels migrated as two bands (total of six bands) with altered electrophoretic mobilities. In experiments using the alkylating agent iodoacetamide under conditions where the novel 24000, 21000 and 17000 polypeptides were not visible, the number of mobility variants of the 23 000 polypeptide which could be detected in non-reducing conditions was increased from two to four. At least one, and possibly three, of these variants was the result of conformational variation in the 23000 polypeptide caused by the generation or rearrangement of intrachain disulphide bonds after the infected cells were lysed in SDS-PAGE sample buffer. Post-lysis conformational changes were minimized by treatment of the infected cells with iodoacetamide before solubilization or by decreasing the SDS concentration or using milder detergents in the lysis buffer.

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“…This reaction was first discussed at some length by Huggins et al (1951), who drew attention to the inevitability of the reaction for proteins that contain both thiol and disulfide groups, particularly in urea solutions where rapid gelling occurs due to intermolecular disulfide bond formation. Surprisingly, few proteins contain both thiol and disulfide groups, ovalbumin being one of the most common examples.…”

Section: Discussionmentioning

confidence: 99%

“…Cystine and cysteine playa significant role in the properties of many proteins, and ovalbumin is one of the readily available proteins that possess both thiol and disulfide bonds. Huggins et al (1951) first drew attention to the thiol-disulfide exchange reaction in proteins that contain both thiol and disulfide groups, particularly in urea solutions, but it was Ryle and Sanger (1955) who emphasized the catalytic effects ofthiol groups in neutral or alkaline solutions. Thiol-disulfide interchange was shown to be minimal in dilute acid solutions (Ryle and Sanger 1955;Spackman et al 1960;Cecil 1963).…”

Section: Introductionmentioning

confidence: 99%

Carboxymethylation of Thiol Groups in Ovalbumin: Implications for Proteins that Contain Both Thiol and Disulfide Groups

Webster¹,

Thompson²

1982

Aust. Jnl. Of Bio. Sci.

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The cysteine residues of hen ovalbumin were S-carboxymethylated with non-radioactive iodoacetic acid under various conditions by altering the pH at which the protein was denatured in 8 M urea, by using different molar ratios of non-radioactive iodoacetic acid to cysteine and by varying the time at which carboxymethylation was commenced after denaturing conditions had been applied. Under the various conditions, the thiol groups were carboxymethylated to different extents, the residual thiol groups being measured by reaction with 5,5'-dithiobis(2-nitrobenzoic acid) in the presence of sodium dodecyl sulfate. When ovalbumin is carboxymethylated in alkaline urea, it unfolds slowly and the carboxymethylation is incomplete even with 150-fold excess iodoacetic acid. The known rapid thiol-disulfide exchange that occurs at alkaline pH values makes this method of carboxymethylation unsuitable as a preliminary step for blocking the native cysteine residues of ovalbumin before reduction and labelling the thiol groups formed by reduction of the disulfide bonds.Titration of the thiol groups of ovalbumin in 6 M guanidine hydrochloride or 1 % (w/v) sodium dodecyl sulfate at pH 8·2 with 5,5' -dithiobis(2-nitrobenzoic acid) is more rapid than in 8 M urea and these solvents would be preferable for studies of the disulfide-bonded sequences. Denaturation of ovalbumin in acidic 8 M urea is a very rapid process, and under mild acid conditions thiol-disulfide interchange is much slower. Subsequent carboxymethylation of the cysteine residues at alkaline pH with 150-fold excess iodoacetic acid results in complete carboxymethylation and the carboxymethylated ovalbumin can be reduced and labelled with radioactive iodoacetic acid with specific labelling of the half-cystine residues involved in the disulfide bond. The results are discussed in relation to the allocation of half-cystine residues in other protein systems that contain both thiol and disulfide groups.

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Sulphydryl-Disulphide Relationships in the Induction of Gels in Proteins by Urea

Cited by 208 publications

References 10 publications

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Heterogeneity of the Respiratory Syncytial Virus 22K Protein Revealed by Western Blotting with Monoclonal Antibodies

Carboxymethylation of Thiol Groups in Ovalbumin: Implications for Proteins that Contain Both Thiol and Disulfide Groups

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