[{
  "type": "article-journal",
  "title": "THE DETECTION AND IDENTIFICATION OF THE CR1-LIKE MEMBRANE BINDING PROTEIN OF PORCINE ERYTHROCYTES",
  "author": [
    {
      "family": "Zhang",
      "given": ""
    },
    {
      "family": "Fan",
      "given": ""
    },
    {
      "family": "Sun",
      "given": ""
    },
    {
      "family": "Sun",
      "given": ""
    },
    {
      "family": "Sun",
      "given": ""
    },
    {
      "family": "Li",
      "given": ""
    },
    {
      "family": "Yin",
      "given": ""
    }
  ],
  "issued": {
    "date-parts": [[2024]]
  },
  "container-title": "Journal of Animal and Plant Sciences",
  "ISSN": "1018-7081",
  "volume": "34",
  "issue": "5",
  "page": "1324-1332",
  "DOI": "https://doi.org/10.36899/JAPS.2024.5.0814",
  "abstract": "<p>Erythrocyte complement receptor I-like (ECR1-like) is a natural immunoreactive molecule on the surface of porcine erythrocyte membrane. The aim of this study was to establish an effective method for the detection and characterization of porcine erythrocyte CR1-like membrane-bound proteins, and to explore their expression characteristics and biological significance in porcine erythrocyte membranes.The CR1-like protein ligands were observed by laser confocal microscopy using fluorescence immunocytochemistry with two types of PDZ-binding domain monoclonal antibodies, FAP-1 (Fas-associated phosphatase-1) and ZO2 (Tight Junction Protein ZO-2); meanwhile, immunoprecipitation and Western blot techniques were used to detect the membrane proteins of porcine blood cells. The immunofluorescence cytochemical staining showed that the specific fluorescence sites of CR1-like and FAP-1 molecules in the porcine erythrocyte membrane skeleton were identical; the sum of the difference squares of the site distances of 253 typical positive erythrocytes was 0.2224, indicating that the difference between the site distances of CR1-like and FAP-1 in each group was approximately 0. The results showed that the distribution of CR1-like and FAP-1 was consistent with a co-local relationship, and the FAP-1 molecule was clearly observed in the examined gel by immunoprecipitation. The results indicate that CR1-like does not bind directly to the erythrocyte membrane skeleton protein, but is distributed on the surface of the porcine erythrocyte membrane through the riveted structure of the FAP-1 protein molecule.</p>",
  "publisher": "Pakistan Agricultural Scientists Forum",
  "URL": "https://thejaps.org.pk/AbstractView.aspx?mid=2023-JAPS-811"
}]