2001
DOI: 10.1017/s0022029901004927
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Effect of pH on antigen-binding activity of IgG from bovine colostrum upon heating

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Cited by 27 publications
(37 citation statements)
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References 15 publications
(48 reference statements)
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“…The conformation change in the IgG molecule occurred during heat exposure reduces antigen-binding activity of this protein Calmettes et al [62], whereas, antigen-binding site of IgG is more sensitive to heat compared to other part of the molecule [21,22]. Trujillo et al [19] reported that Immunoglobulins, are species specific on heat sensitivity particularly IgG such as on bovine, caprine and ovine.…”
Section: Effect Of Heat On Liquid Whey Igg Content At Various Phmentioning
confidence: 99%
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“…The conformation change in the IgG molecule occurred during heat exposure reduces antigen-binding activity of this protein Calmettes et al [62], whereas, antigen-binding site of IgG is more sensitive to heat compared to other part of the molecule [21,22]. Trujillo et al [19] reported that Immunoglobulins, are species specific on heat sensitivity particularly IgG such as on bovine, caprine and ovine.…”
Section: Effect Of Heat On Liquid Whey Igg Content At Various Phmentioning
confidence: 99%
“…high stability in a decreasing order from IgG, IgA and IgM as well as varies among species [17][18][19]. The conformation changes in the IgG molecule which occurs during heat exposure reduces antigen-binding activity of this protein Calmettes et al [20] and antigen-binding site of IgG is more sensitive to heat compared to other part of the molecule [21,22]. On the other hand, LF are denatured by heat treatment too, therefore pasteurizing milk might affect LF unless mild heat treatment is applied [23,24].…”
Section: Introductionmentioning
confidence: 99%
“…Immunoglobulins are among the most heat-stable whey proteins, though this varies with the subtype (IgG being the most resistant) (Dominguez et al 2001). Retention of their bioactivity post-processing is of concern, however, due to their potential denaturation and loss of associated beneficial functions.…”
Section: Immunoglobulins and Colostrummentioning
confidence: 99%
“…pH 4.5). However, this effect may be less severe when in the presence of milk or colostrum, likely due to inherent protection by milk proteins and salts (Dominguez et al 2001). Chen et al (2000) found that milk IgG could be significantly stabilized during heat processing when in the presence of 20% glycerol, 20% maltose, or 0.2% glutamic acid.…”
Section: Immunoglobulins and Colostrummentioning
confidence: 99%
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