메뉴 건너뛰기




Volumn 245, Issue 2, 1996, Pages 201-208

Degradation of glycated hemoglobin by erythrocytic proteolytic enzymes

Author keywords

Diabetes mellitus; Erythrocytes; Glycated hemoglobin; Proteolytic enzymes

Indexed keywords

GLYCOSYLATED HEMOGLOBIN; HEMOGLOBIN;

EID: 0029944522     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/0009-8981(95)06185-1     Document Type: Article
Times cited : (6)

References (24)
  • 1
    • 0023110924 scopus 로고
    • The relative extent of glycation of hemoglobin and albumin
    • Olufemi S, Talwar D, Robb DA. The relative extent of glycation of hemoglobin and albumin. Clin Chim Acta 1987;163:125-136.
    • (1987) Clin Chim Acta , vol.163 , pp. 125-136
    • Olufemi, S.1    Talwar, D.2    Robb, D.A.3
  • 3
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification: The potential role of autoxidative glycosylation in diabetes
    • Wolf SP, Dean RT. Glucose autoxidation and protein modification: the potential role of autoxidative glycosylation in diabetes. Biochem J 1987;245:243-250.
    • (1987) Biochem J , vol.245 , pp. 243-250
    • Wolf, S.P.1    Dean, R.T.2
  • 4
    • 0023755121 scopus 로고
    • Superoxide production from non-enzymatically glycated protein
    • Sakurai T, Tsuchiya S. Superoxide production from non-enzymatically glycated protein. Fed Eur Biochem Soc Lett 1988;236:406-410.
    • (1988) Fed Eur Biochem Soc Lett , vol.236 , pp. 406-410
    • Sakurai, T.1    Tsuchiya, S.2
  • 5
    • 0023708392 scopus 로고
    • Hydroxyl radical production and autoxidative glycosylation
    • Hunt JV, Dean RT, Wolf SP. Hydroxyl radical production and autoxidative glycosylation. Biochem J 1988;256:205-212.
    • (1988) Biochem J , vol.256 , pp. 205-212
    • Hunt, J.V.1    Dean, R.T.2    Wolf, S.P.3
  • 6
    • 0024311551 scopus 로고
    • Impairment of glutathione metabolism in erythrocytes from patients with diabetes mellitus
    • Murakami KK, Kondo T, Ohtsuka Y, Fujiwara Y, Shimada M, Kawakami Y. Impairment of glutathione metabolism in erythrocytes from patients with diabetes mellitus. Metabolism 1989;38:753-758.
    • (1989) Metabolism , vol.38 , pp. 753-758
    • Murakami, K.K.1    Kondo, T.2    Ohtsuka, Y.3    Fujiwara, Y.4    Shimada, M.5    Kawakami, Y.6
  • 7
    • 0026056573 scopus 로고
    • Reduced vitamin E and increased lipofuscin products in erythrocytes of diabetic rats
    • Jain SK, Levine SN, Duett J, Hollier B. Reduced vitamin E and increased lipofuscin products in erythrocytes of diabetic rats. Diabetes 1991;40:1241-1244.
    • (1991) Diabetes , vol.40 , pp. 1241-1244
    • Jain, S.K.1    Levine, S.N.2    Duett, J.3    Hollier, B.4
  • 8
    • 0026482202 scopus 로고
    • Clinical significance of SOD changes in aging, diabetes, ischaemia and cancer
    • Taniguchi N. Clinical significance of SOD changes in aging, diabetes, ischaemia and cancer. Adv Clin Chem 1992;29:1-59.
    • (1992) Adv Clin Chem , vol.29 , pp. 1-59
    • Taniguchi, N.1
  • 9
    • 0343288439 scopus 로고
    • Red blood cells contain a pathway for the degradation of oxidant damaged hemoglobin that does not require ATP or ubiquitin
    • Fagan JM, Waxman L, Goldberg AL. Red blood cells contain a pathway for the degradation of oxidant damaged hemoglobin that does not require ATP or ubiquitin. J Biol Chem 1987;262:8220-8226.
    • (1987) J Biol Chem , vol.262 , pp. 8220-8226
    • Fagan, J.M.1    Waxman, L.2    Goldberg, A.L.3
  • 10
    • 0023655050 scopus 로고
    • Proteins damaged by oxygen radicals are rapidly degraded by RBC extracts
    • Davies KJA, Goldberg AL. Proteins damaged by oxygen radicals are rapidly degraded by RBC extracts. J Biol Chem 1987;262:8227-8234.
    • (1987) J Biol Chem , vol.262 , pp. 8227-8234
    • Davies, K.J.A.1    Goldberg, A.L.2
  • 11
    • 0020536066 scopus 로고
    • Effect of saline incubation on red cell content of glucosylated hemoglobins studied by iso-electric focusing
    • Mortensen HB, Marshall MO. Effect of saline incubation on red cell content of glucosylated hemoglobins studied by iso-electric focusing. Clin Chim Acta 1983;132:213-217.
    • (1983) Clin Chim Acta , vol.132 , pp. 213-217
    • Mortensen, H.B.1    Marshall, M.O.2
  • 12
    • 0019442781 scopus 로고
    • Rapid glycosylation of hemoglobin
    • Paisey R. Rapid glycosylation of hemoglobin. Diabetologia 1981;20:80.
    • (1981) Diabetologia , vol.20 , pp. 80
    • Paisey, R.1
  • 13
    • 0028297867 scopus 로고
    • Increased proteolysis of oxidatively damaged hemoglobin in erythrocyte lysates in diabetes mellitus
    • Raghothama C, Rao P. Increased proteolysis of oxidatively damaged hemoglobin in erythrocyte lysates in diabetes mellitus. Clin Chim Acta 1994;225:65-70.
    • (1994) Clin Chim Acta , vol.225 , pp. 65-70
    • Raghothama, C.1    Rao, P.2
  • 14
    • 0015230826 scopus 로고
    • Hemoglobin components in patients with diabetes mellites
    • Trivelli LA, Ranney HM, Lai HT. Hemoglobin components in patients with diabetes mellites. N Engl J Med 1971;284:353-357.
    • (1971) N Engl J Med , vol.284 , pp. 353-357
    • Trivelli, L.A.1    Ranney, H.M.2    Lai, H.T.3
  • 16
    • 0018747526 scopus 로고
    • Generation of Superoxide radicals by hydrazine; its role in phenylhydrazine induced hemolytic anaemia
    • Jain SK, Hochstein P. Generation of Superoxide radicals by hydrazine; its role in phenylhydrazine induced hemolytic anaemia. Biochim Biophys Acta 1979;586:128-136.
    • (1979) Biochim Biophys Acta , vol.586 , pp. 128-136
    • Jain, S.K.1    Hochstein, P.2
  • 17
    • 0026468409 scopus 로고
    • The ATP-independent pathway in red blood cells that degrades oxidant damaged hemoglobin
    • Fagan JM, Waxman L. The ATP-independent pathway in red blood cells that degrades oxidant damaged hemoglobin. J Biol Chem 1992;267:23015-23022.
    • (1992) J Biol Chem , vol.267 , pp. 23015-23022
    • Fagan, J.M.1    Waxman, L.2
  • 18
    • 0020669405 scopus 로고
    • Determination of total protein
    • Peterson GL. Determination of total protein. Methods Enzymol 1983;91:95-119.
    • (1983) Methods Enzymol , vol.91 , pp. 95-119
    • Peterson, G.L.1
  • 19
    • 0022381534 scopus 로고
    • Autoxidation reactions of hemoglobin A free from other red cell components: A minimal mechanism
    • Watkins JA, Kawanishi S, Caughey WS. Autoxidation reactions of hemoglobin A free from other red cell components: a minimal mechanism. Biochem Biophys Res Commun 1985;132:742-748.
    • (1985) Biochem Biophys Res Commun , vol.132 , pp. 742-748
    • Watkins, J.A.1    Kawanishi, S.2    Caughey, W.S.3
  • 22
    • 0026810263 scopus 로고
    • 1c upon return to normoglycemia
    • 1c upon return to normoglycemia [letter]. Diabetologia 1992;35;191.
    • (1992) Diabetologia , vol.35 , pp. 191
    • Chantelau, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.