1970
DOI: 10.1111/j.1432-1033.1970.tb00291.x
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Large Scale Isolation, Characterization and Classification of Pig Immunoglobulin k-Chains

Abstract: The χ‐chains were prepared by chromatography and rechromatography of pig S‐sulfo‐immunoglobulin on Sephadex G‐100 and SE‐Sephadex, and characterized by starch‐gel electro‐phoresis, amino acid analysis, molecular weight (25000 ± 2500) and N‐terminal amino acid (alanine). From the tryptic digest of the χ‐chains, the N‐terminal tetracosapeptide was isolated and its amino acid sequence determined as These results provide evidence of the similarity between pig immunoglobulin χ‐chains and the human and mouse type… Show more

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Cited by 13 publications
(3 citation statements)
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“…The overall pattern of amino acid variability of pooled nonspecific porcine chains resembles closely that found with some murine chains (Weigert et al, 1970); i.e., they possess almost constant framework regions and highly variable complementarity regions. This is in marked contrast to the variability pattern of pooled equine chains (Gibson, 1974) and porcine chains (Novotny et al, 1970) in which N-proximal framework regions display significant variability.…”
Section: Discussioncontrasting
confidence: 84%
“…The overall pattern of amino acid variability of pooled nonspecific porcine chains resembles closely that found with some murine chains (Weigert et al, 1970); i.e., they possess almost constant framework regions and highly variable complementarity regions. This is in marked contrast to the variability pattern of pooled equine chains (Gibson, 1974) and porcine chains (Novotny et al, 1970) in which N-proximal framework regions display significant variability.…”
Section: Discussioncontrasting
confidence: 84%
“…The conclusions presented in this paper are based on experiments in which either pig immunoglobulin polypeptide chains or peptides from tryptic digest of pig immunoglobulin K chains were fractionated on SE-(sulfoethyl)-Sephadex C-25 and QAE-(quaternized aminoethyl)-Sephadex A-25 [6,7]. The following North-Holland Publishing Company -Amsterdam buffers were used: chromatography on SE-Sephadex: 5 mM potassium formate, 8 M in urea, adjusted to pH 3.0 with formic acid; chromatography on QAE-Sephadex: 0.01 M sodium acetate, 8 M in urea, adjusted to pH 5.0 with acetic acid.…”
Section: Methodsmentioning
confidence: 99%
“…The conclusions presented in this paper are based on experiments in which either pig immunoglobulin polypeptide chains or peptides from tryptic digest of pig immunoglobulin K chains were fractionated on SE-(sulfoethyl)-Sephadex C-25 and QAE-(quaternized aminoethyl)-Sephadex A-25 [6,7]. The following fig.…”
Section: Methodsmentioning
confidence: 99%