Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells

Ichiro Tokimitsu, Makoto Takehana, Hisae Hori, Yutaka Nagai, Shingo Tajima

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Two collagenous polypeptides with apparent molecular weights of 180 and 500 kDa under a nonreducing condition were found to be produced in the culture medium of B16 mouse melanoma cells. Under a reducing condition, the higher molecular weight polypeptide (500 kDa) migrated at an identical position to the 180 kDa polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both polypeptides were found to have an identical primary structure by V8 protease peptide mapping. Cyanogen bromide cleavage patterns, the fragments produced by pepsin digestion, and partial amino acid sequences of the 180 kDa polypeptide were compatible with those of proα1(IV) chain. These results indicate that B16 mouse melanoma cells preferentially produce proα1(IV) chains consisting of two forms: disulfide- and nondisulfide-bonded forms.

Original languageEnglish
Pages (from-to)1039-1043
Number of pages5
JournalJournal of Biochemistry
Volume116
Issue number5
Publication statusPublished - 1994 Nov

Fingerprint

Melanoma
Experimental Melanomas
Polypeptides
Mouse
Peptides
Protease
Cell
Amino Acid Sequence
Electrophoresis
Sodium
Fragment
Partial
Molecular Weight
Molecular weight
Cyanogen Bromide
Peptide Mapping
Pepsin A
Sodium dodecyl sulfate
Polyacrylates
Sodium Dodecyl Sulfate

Keywords

  • B16 mouse melanoma
  • Type IV collagen

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Tokimitsu, I., Takehana, M., Hori, H., Nagai, Y., & Tajima, S. (1994). Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells. Journal of Biochemistry, 116(5), 1039-1043.

Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells. / Tokimitsu, Ichiro; Takehana, Makoto; Hori, Hisae; Nagai, Yutaka; Tajima, Shingo.

In: Journal of Biochemistry, Vol. 116, No. 5, 11.1994, p. 1039-1043.

Research output: Contribution to journalArticle

Tokimitsu, I, Takehana, M, Hori, H, Nagai, Y & Tajima, S 1994, 'Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells', Journal of Biochemistry, vol. 116, no. 5, pp. 1039-1043.
Tokimitsu I, Takehana M, Hori H, Nagai Y, Tajima S. Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells. Journal of Biochemistry. 1994 Nov;116(5):1039-1043.
Tokimitsu, Ichiro ; Takehana, Makoto ; Hori, Hisae ; Nagai, Yutaka ; Tajima, Shingo. / Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells. In: Journal of Biochemistry. 1994 ; Vol. 116, No. 5. pp. 1039-1043.
@article{391b899e394c418e98bdc706f137419a,
title = "Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells",
abstract = "Two collagenous polypeptides with apparent molecular weights of 180 and 500 kDa under a nonreducing condition were found to be produced in the culture medium of B16 mouse melanoma cells. Under a reducing condition, the higher molecular weight polypeptide (500 kDa) migrated at an identical position to the 180 kDa polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both polypeptides were found to have an identical primary structure by V8 protease peptide mapping. Cyanogen bromide cleavage patterns, the fragments produced by pepsin digestion, and partial amino acid sequences of the 180 kDa polypeptide were compatible with those of proα1(IV) chain. These results indicate that B16 mouse melanoma cells preferentially produce proα1(IV) chains consisting of two forms: disulfide- and nondisulfide-bonded forms.",
keywords = "B16 mouse melanoma, Type IV collagen",
author = "Ichiro Tokimitsu and Makoto Takehana and Hisae Hori and Yutaka Nagai and Shingo Tajima",
year = "1994",
month = "11",
language = "English",
volume = "116",
pages = "1039--1043",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "5",

}

TY - JOUR

T1 - Identification of nondisulfided proα1(IV) chain produced by cultured B16 melanoma cells

AU - Tokimitsu, Ichiro

AU - Takehana, Makoto

AU - Hori, Hisae

AU - Nagai, Yutaka

AU - Tajima, Shingo

PY - 1994/11

Y1 - 1994/11

N2 - Two collagenous polypeptides with apparent molecular weights of 180 and 500 kDa under a nonreducing condition were found to be produced in the culture medium of B16 mouse melanoma cells. Under a reducing condition, the higher molecular weight polypeptide (500 kDa) migrated at an identical position to the 180 kDa polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both polypeptides were found to have an identical primary structure by V8 protease peptide mapping. Cyanogen bromide cleavage patterns, the fragments produced by pepsin digestion, and partial amino acid sequences of the 180 kDa polypeptide were compatible with those of proα1(IV) chain. These results indicate that B16 mouse melanoma cells preferentially produce proα1(IV) chains consisting of two forms: disulfide- and nondisulfide-bonded forms.

AB - Two collagenous polypeptides with apparent molecular weights of 180 and 500 kDa under a nonreducing condition were found to be produced in the culture medium of B16 mouse melanoma cells. Under a reducing condition, the higher molecular weight polypeptide (500 kDa) migrated at an identical position to the 180 kDa polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both polypeptides were found to have an identical primary structure by V8 protease peptide mapping. Cyanogen bromide cleavage patterns, the fragments produced by pepsin digestion, and partial amino acid sequences of the 180 kDa polypeptide were compatible with those of proα1(IV) chain. These results indicate that B16 mouse melanoma cells preferentially produce proα1(IV) chains consisting of two forms: disulfide- and nondisulfide-bonded forms.

KW - B16 mouse melanoma

KW - Type IV collagen

UR - http://www.scopus.com/inward/record.url?scp=0028171438&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028171438&partnerID=8YFLogxK

M3 - Article

C2 - 7896731

AN - SCOPUS:0028171438

VL - 116

SP - 1039

EP - 1043

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 5

ER -