DOI: 10.4049/jimmunol.131.4.1876. Biosynthesis, glycosylation, and <i>in vitro</i> translation of the human T cell antigen Leu-4.

Biosynthesis, glycosylation, and in vitro translation of the human T cell antigen Leu-4.

10.4049/jimmunol.131.4.1876

Crossref journal-article

Oxford University Press (OUP)

The Journal of Immunology (286)

Abstract

Abstract Two families of polypeptides were found in immunoprecipitates formed from human T cell lines by using the monoclonal antibody anti-Leu-4. When analyzed by one- and two-dimensional SDS-PAGE, the first family consisted of members with m.w. of 26,000 and isoelectric points that varied from very basic to acidic. The second family consisted of members with m.w. of 22,000 to 23,000 and isolectric points that varied from neutral to very acidic. The biosynthetic processing and intracellular glycosylation of several of these polypeptides were examined. Some, but not all, intracellular forms of the Leu-4 antigen contained N-linked oligosaccharides of the high mannose type. By using messenger RNA from human T cell lines, intracellular forms of Leu-4 were shown to be accurately translated and properly processed by Xenopus oocytes in vitro.

Bibliography

Bergman, Y., Stewart, S. J., Levy, S., & Levy, R. (1983). Biosynthesis, glycosylation, and in vitro translation of the human T cell antigen Leu-4. The Journal of Immunology, 131(4), 1876â1881.

Authors 4

Y Bergman (first)
S J Stewart (additional)
S Levy (additional)
R Levy (additional)

References 0 Referenced 19

None

Dates

Type	When
Created	2 years, 8 months ago (Dec. 30, 2022, 9:04 p.m.)
Deposited	5 months ago (March 31, 2025, 6:42 p.m.)
Indexed	2 months, 2 weeks ago (June 20, 2025, 2:44 p.m.)
Issued	41 years, 11 months ago (Oct. 1, 1983)
Published	41 years, 11 months ago (Oct. 1, 1983)
Published Online	41 years, 11 months ago (Oct. 1, 1983)
Published Print	41 years, 11 months ago (Oct. 1, 1983)

Funders 0

None

BibTeX

@article{Bergman_1983, title={Biosynthesis, glycosylation, and in vitro translation of the human T cell antigen Leu-4.}, volume={131}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.131.4.1876}, DOI={10.4049/jimmunol.131.4.1876}, number={4}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Bergman, Y and Stewart, S J and Levy, S and Levy, R}, year={1983}, month=oct, pages={1876–1881} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        6,
        20
      ]
    ],
    "date-time": "2025-06-20T18:44:13Z",
    "timestamp": 1750445053037,
    "version": "3.40.3"
  },
  "reference-count": 0,
  "publisher": "Oxford University Press (OUP)",
  "issue": "4",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            1983,
            10,
            1
          ]
        ],
        "date-time": "1983-10-01T00:00:00Z",
        "timestamp": 433814400000
      },
      "content-version": "vor",
      "delay-in-days": 0,
      "URL": "https://academic.oup.com/pages/standard-publication-reuse-rights"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1983,
        10,
        1
      ]
    ]
  },
  "abstract": "<jats:title>Abstract</jats:title>\n               <jats:p>Two families of polypeptides were found in immunoprecipitates formed from human T cell lines by using the monoclonal antibody anti-Leu-4. When analyzed by one- and two-dimensional SDS-PAGE, the first family consisted of members with m.w. of 26,000 and isoelectric points that varied from very basic to acidic. The second family consisted of members with m.w. of 22,000 to 23,000 and isolectric points that varied from neutral to very acidic. The biosynthetic processing and intracellular glycosylation of several of these polypeptides were examined. Some, but not all, intracellular forms of the Leu-4 antigen contained N-linked oligosaccharides of the high mannose type. By using messenger RNA from human T cell lines, intracellular forms of Leu-4 were shown to be accurately translated and properly processed by Xenopus oocytes in vitro.</jats:p>",
  "DOI": "10.4049/jimmunol.131.4.1876",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2022,
        12,
        31
      ]
    ],
    "date-time": "2022-12-31T02:04:11Z",
    "timestamp": 1672452251000
  },
  "page": "1876-1881",
  "source": "Crossref",
  "is-referenced-by-count": 19,
  "title": "Biosynthesis, glycosylation, and <i>in vitro</i> translation of the human T cell antigen Leu-4.",
  "prefix": "10.1093",
  "volume": "131",
  "author": [
    {
      "given": "Y",
      "family": "Bergman",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Department of Medicine, Stanford University , Stanford, CA 94305"
        }
      ]
    },
    {
      "given": "S J",
      "family": "Stewart",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Medicine, Stanford University , Stanford, CA 94305"
        }
      ]
    },
    {
      "given": "S",
      "family": "Levy",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Life Sciences Division, SRI International , 333 Ravenswood Avenue, Menlo Park, CA 94025"
        }
      ]
    },
    {
      "given": "R",
      "family": "Levy",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Medicine, Stanford University , Stanford, CA 94305"
        }
      ]
    }
  ],
  "member": "286",
  "published-online": {
    "date-parts": [
      [
        1983,
        10,
        1
      ]
    ]
  },
  "container-title": "The Journal of Immunology",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://academic.oup.com/jimmunol/article-pdf/131/4/1876/62797245/1876.pdf",
      "content-type": "application/pdf",
      "content-version": "vor",
      "intended-application": "syndication"
    },
    {
      "URL": "https://academic.oup.com/jimmunol/article-pdf/131/4/1876/62797245/1876.pdf",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2025,
        3,
        31
      ]
    ],
    "date-time": "2025-03-31T22:42:16Z",
    "timestamp": 1743460936000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://academic.oup.com/jimmunol/article/131/4/1876/8073274"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1983,
        10,
        1
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "4",
    "published-print": {
      "date-parts": [
        [
          1983,
          10,
          1
        ]
      ]
    }
  },
  "URL": "http://dx.doi.org/10.4049/jimmunol.131.4.1876",
  "relation": {},
  "ISSN": [
    "0022-1767",
    "1550-6606"
  ],
  "subject": [],
  "published-other": {
    "date-parts": [
      [
        1983,
        10
      ]
    ]
  },
  "published": {
    "date-parts": [
      [
        1983,
        10,
        1
      ]
    ]
  }
}