Developmental changes in membrane proteins from baboon erythrocytes

John C. Lee; Thomas J. Kuehl; G. David Roodman

doi:10.1016/0305-0491(87)90106-4

Developmental changes in membrane proteins from baboon erythrocytes

John C. Lee, Thomas J. Kuehl, G. David Roodman

Biochemistry & Structural Biology

Research output: Contribution to journal › Article

Abstract

1. 1. Total membrane proteins from freshly isolated erythrocytes of fetal, newborn, and adult baboons were analyzed by electrophoresis. 2. 2. The electrophoretic patterns of proteins from newborns and adults were similar but those from adults and fetuses were different. 3. 3. Four proteins, P₁₆₅, P₁₅₅, P₇₅, and P₄₉, with approximate mol. wts of 165,000, 155,000, 75,000, and 49,000, respectively, were present in adult but not in fetal samples. 4. 4. P₁₅₅ and P₄₉, were glycoproteins; P₄₉ was a cell-surface protein. 5. 5. The membrane protein characteristics of the adult erythrocyte differ from those of the fetal erythrocytes and at least four polypeptides are associated with development of the adult phenotype.

Original language	English (US)
Pages (from-to)	233-236
Number of pages	4
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	88
Issue number	1
DOIs	https://doi.org/10.1016/0305-0491(87)90106-4
State	Published - 1987

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ASJC Scopus subject areas

Biochemistry
Physiology
Molecular Biology

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Lee, J. C., Kuehl, T. J., & Roodman, G. D. (1987). Developmental changes in membrane proteins from baboon erythrocytes. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 88(1), 233-236. https://doi.org/10.1016/0305-0491(87)90106-4

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abstract = "1. 1. Total membrane proteins from freshly isolated erythrocytes of fetal, newborn, and adult baboons were analyzed by electrophoresis. 2. 2. The electrophoretic patterns of proteins from newborns and adults were similar but those from adults and fetuses were different. 3. 3. Four proteins, P165, P155, P75, and P49, with approximate mol. wts of 165,000, 155,000, 75,000, and 49,000, respectively, were present in adult but not in fetal samples. 4. 4. P155 and P49, were glycoproteins; P49 was a cell-surface protein. 5. 5. The membrane protein characteristics of the adult erythrocyte differ from those of the fetal erythrocytes and at least four polypeptides are associated with development of the adult phenotype.",

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N2 - 1. 1. Total membrane proteins from freshly isolated erythrocytes of fetal, newborn, and adult baboons were analyzed by electrophoresis. 2. 2. The electrophoretic patterns of proteins from newborns and adults were similar but those from adults and fetuses were different. 3. 3. Four proteins, P165, P155, P75, and P49, with approximate mol. wts of 165,000, 155,000, 75,000, and 49,000, respectively, were present in adult but not in fetal samples. 4. 4. P155 and P49, were glycoproteins; P49 was a cell-surface protein. 5. 5. The membrane protein characteristics of the adult erythrocyte differ from those of the fetal erythrocytes and at least four polypeptides are associated with development of the adult phenotype.

AB - 1. 1. Total membrane proteins from freshly isolated erythrocytes of fetal, newborn, and adult baboons were analyzed by electrophoresis. 2. 2. The electrophoretic patterns of proteins from newborns and adults were similar but those from adults and fetuses were different. 3. 3. Four proteins, P165, P155, P75, and P49, with approximate mol. wts of 165,000, 155,000, 75,000, and 49,000, respectively, were present in adult but not in fetal samples. 4. 4. P155 and P49, were glycoproteins; P49 was a cell-surface protein. 5. 5. The membrane protein characteristics of the adult erythrocyte differ from those of the fetal erythrocytes and at least four polypeptides are associated with development of the adult phenotype.

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10.1016/0305-0491(87)90106-4