Crossed Immunoelectrophoresis

Ganrot, P. O.

doi:10.3109/00365517209102749

Cited by 301 publications

(57 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The 35 samples from days 1, 2, and 3 with a protease inhibiting activity had no, or low, caseinolytic activity. Samples from day 4 or later had no, or low caseinolytic and elastinolytic activity. Figure 4 shows that the caseinolytic activity in human milk was present in a broad region with a Pmobility in agarose gel electrophoresis.…”

Section: I L K 1215mentioning

confidence: 99%

Protease Inhibitors and their Relation to Protease Activity in Human Milk

1982

View full text Add to dashboard Cite

Section: I L K 1215mentioning

confidence: 99%

Protease Inhibitors and their Relation to Protease Activity in Human Milk

1982

View full text Add to dashboard Cite

“…Agarose gel electrophoresis (I 8), crossed immunoelectrophoresis (13,23), and electroimmunoassay (24,25) were performed with 0.075 M barbital-sodium barbitaibuffer, pH 8.6, containing 0.002 M calcium lactate.…”

Section: Electrophoresis a N D Immunoelectrophoresismentioning

confidence: 99%

Protease Inhibitors in Human Milk

Lindberg

1979

Pediatr Res

View full text Add to dashboard Cite

Summarystandard serum for the measurements of the concentration of a,-Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the al-region-inhibiting trypsin, chymotrypsin, and elastase-and in a more cathodal region-inhibiting chymotrypsin-in agarose gel electrophoresis of human milk. alantitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of a,-antitrypsin in 1st day milk to be 109% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations d&;eased during the 1st wk; from 1 wk to 4 months they were 1.6% for a,-antitrypsin and 3.84% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0-150 pg (mean value, 70 pg) trypsin. Milk from 1 week after delivery and later inhibits 0-65 pg (mean value, 38 pg) trypsin per ml.

show abstract

“…Monospecific rabbit antisera were used to detect Factor XIII in all extracts by crossed immunoelectrophoresis (30). It had previously been determined that anti-A reacted only with A and not B, and anti-B reacted only with B and not A (31,32 …”

Section: Introductionmentioning

confidence: 99%

Identification of intracellular factor XIII in human monocytes and macrophages.

Henriksson¹,

Becker²,

Lynch³

et al. 1985

J. Clin. Invest.

159

View full text Add to dashboard Cite

Factor XIII is a blood protransglutaminase that is distributed in plasma and platelets. The extracellular and intracellular zymogenic forms differ in that the plasma zymogen contains A and B subunits, while the platelet zymogen has A subunits only. Both zymogens form the same enzyme. Erythrocytes, in contrast, contain a tissue transglutaminase that is distinct from Factor XIII. In this study other bone marrow-derived cells were examined for transglutaminase activity. Criteria that were used to differentiate Factor XIII proteins from erythrocyte transglutaminase included: (a) immunochemical and immunohistochemical identification with monospecific polyclonal and monoclonal antibodies to Factor XIII proteins, (b) requirement for thrombin cleavage to express activity, (c) pattern of fibrin cross-linking catalyzed by the enzyme, and (d) different electrophoretic mobilities in nondenaturing gel systems. By these criteria human peripheral blood monocytes, peritoneal macrophages, and monocytes maintained in culture contain an intracellular protransglutaminase that is the same as platelet Factor XIII. The monocyte-macrophage protein is thrombin-sensitive, and under appropriate conditions there is no enzyme expression without activation of the zymogen. Both the monocyte-macrophage zymogen and enzyme have the same electrophoretic mobilities as platelet Factor XIII zymogen and enzyme. Antibody to A protein reacts with the monocyte-macrophage protein. B protein is not associated with this intracellular zymogen. By immunoperoxidase staining monocyte-macrophage protein seems to be localized in the cytoplasm, similar to the known cytoplasmic distribution of platelet and megakaryocyte Factor XIII. These procedures were also used to study populations of human granulocytes and lymphocytes, and protransglutaminase activity was not observed in these cells.

show abstract

Crossed Immunoelectrophoresis

Cited by 301 publications

References 10 publications

Protease Inhibitors and their Relation to Protease Activity in Human Milk

Protease Inhibitors and their Relation to Protease Activity in Human Milk

Protease Inhibitors in Human Milk

Identification of intracellular factor XIII in human monocytes and macrophages.

Contact Info

Product

Resources

About