Studies on the Synthesis of Insulin from Natural and Synthetic A and B Chains. III. Synthetic Insulins<sup>*</sup>

Katsoyannis, Panayotis G.; Trakatellis, Anthony C.; Zalut, Clyde; Stanley, J.; Tometsko, Andrew M.; Schwartz, Gerald; Ginos, James Z.

doi:10.1021/bi00861a003

Cited by 76 publications

(81 citation statements)

References 29 publications

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“…Several methods have been used in other laboratories to facilitate the correct disulfide bond formation (23,38). Saxena and Wetlaufer (24) showed that a mixture of oxidized and reduced glutathione accelerated the reformation of active lysozyme.…”

mentioning

confidence: 99%

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Wampler¹,

Lehman²,

Boger³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Hepatitis B surface antigen (HBsAg) has been extracted from yeast cells that produce HBsAg. These cells contain the gene for surface antigen carried on a plasmid that replicates in the cells. Analysis of the yeast-derived HBsAg by sucrose gradient centrifugation and by polyacrylamide gel electrophoresis shows that the antigen that is initially released from yeast cells is a high molecular weight aggregate of the fundamental Mr 25,000 subunit. Unlike HBsAg derived from human plasma, the yeast antigen is held together by noncovalent interactions and can be dissociated in 2% NaDodSO4 without the use of reducing agents. During in vitro purification of the yeast antigen, some disulfide bonds form spontaneously between the antigen subunits, resulting in a particle composed of a mixture of monomers and disulfide-bonded dimers. Treatment with 3 M thiocyanate converts the 20-nm particles into a fully disulfide-bonded form that is not disrupted in NaDodSO4 unless a reducing agent is added. This disulfidebonded particle resembles the naturally occurring, plasmaderived surface antigen particle, and the in vitro formed particle has been used to prepare a vaccine for humans against hepatitis B virus infection.

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mentioning

confidence: 99%

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Wampler¹,

Lehman²,

Boger³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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“…The homogeneity of the synthetic chains was established by ion-exchange chromatography and thin-layer electrophoresis. Hybrids were constructed by combination of the sulfhydryl forms of the A chain of insulin or A27 insulin with the S-sulfonated forms of the B chain of insulin or synthetic IGF-I at pH 10.5 in the presence of thiols, according to the procedures used previously for the synthesis of insulin analogues (17). The hybrid molecules were homogeneous by isoelectric focusing and/or reversed-phase high-performance liquid chromatography (ref.…”

mentioning

confidence: 99%

Hybrid molecules containing the B-domain of insulin-like growth factor I are recognized by carrier proteins of the growth factor.

Vroede¹,

Rechler²,

Nissley³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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The insulin-like growth factors (IGFs) are polypeptides in plasma that are chemically related to insulin and have mitogenic and insulin-like activity. Unlike insulin, the IGFs circulate in plasma bound to specific high molecular weight carrier proteins that regulate their delivery to target tissues. To define the sites on the IGFs that allow them to be recognized by carrier proteins, we constructed hybrid molecules containing different portions of the insulin, IGF-I, and IGF-II molecules.

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“…This modification is irreversible. However, Ssulfonation is reversible [7] and the re agents, sulfite and tetrathionate ions, are nontoxic. We will report the reconversion of S-GG into the original GG in vivo in a further paper.…”

Section: Discussionmentioning

confidence: 99%

Development of an Intravenous γ-Globulin with Fc Activities

Masuho¹,

Tomibe²,

Matsuzawa³

et al. 1977

Vox Sanguinis

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S-sulfonated γ-globulin (S-GG) was prepared by treating γ-globulin with sulfite and tetrathionate ions. About four interchain disulfide bonds were selectively cleaved to give S-sulfonate groups. Although the above treatment strongly suppresses anticomplementary activity and nonspecific skin reactivity, the resulting S-GG retains high antibody activity. Furthermore, S-GG was found to maintain satisfactory levels for prolonged periods in vivo. The physicochemical and antigenic analyses of S-GG suggest that the S-sulfonation induces structural modification only at restricted sites.

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Studies on the Synthesis of Insulin from Natural and Synthetic A and B Chains. III. Synthetic Insulins^*

Cited by 76 publications

References 29 publications

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Hybrid molecules containing the B-domain of insulin-like growth factor I are recognized by carrier proteins of the growth factor.

Development of an Intravenous γ-Globulin with Fc Activities

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Studies on the Synthesis of Insulin from Natural and Synthetic A and B Chains. III. Synthetic Insulins*

Cited by 76 publications

References 29 publications

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Multiple chemical forms of hepatitis B surface antigen produced in yeast.

Hybrid molecules containing the B-domain of insulin-like growth factor I are recognized by carrier proteins of the growth factor.

Development of an Intravenous γ-Globulin with Fc Activities

Contact Info

Product

Resources

About

Studies on the Synthesis of Insulin from Natural and Synthetic A and B Chains. III. Synthetic Insulins^*