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Isolation and partial sequence analysis of rat basic somatomedin

J S Rubin, I Mariz, J W Jacobs

    Endocrinology
    |March 1, 1982
    PubMed
    Summary
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    Researchers developed an improved method to purify rat basic somatomedin (Sm), a growth factor. This purification confirmed its structural similarity to human insulin-like growth factor I.

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Molecular Biology

    Background:

    • Basic somatomedin (Sm) plays a crucial role in growth and metabolism.
    • Previous studies suggested homology between rat basic Sm and human insulin-like growth factor I (IGF-I).

    Purpose of the Study:

    • To develop an improved purification scheme for rat basic somatomedin (Sm).
    • To structurally characterize purified rat basic Sm and confirm its homology with human IGF-I.

    Main Methods:

    • Utilized Amicon hollow fiber diafiltration for large-scale serum processing.
    • Employed narrow pH range isoelectric focusing to separate Sm from complement components.
    • Applied carboxymethyl-cellulose and Sephadex chromatography for purification.

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    Main Results:

    • Achieved a 100-fold purification of rat basic Sm with approximately 65% activity recovery.
    • The final product met purity criteria through various analyses.
    • Structural analysis revealed striking similarity between amino-terminal sequences of rat basic Sm and human IGF-I.

    Conclusions:

    • The improved purification method is efficient and yields high-purity rat basic Sm.
    • Structural data strongly support the homology between rat basic Sm and human IGF-I.
    • This finding reinforces the conserved nature of IGFs across species.