… Joe Beavo and David Reifsnyder summrize much of the evidence that hns led to oldr current
understanding of multipIe isozyrnes of phosphodiesterczse, with emphasis on aspects thnt …

We have identified and highly purified a “low Km” CAMP phos-phodiesterase from bovine
cardiac muscle. This phosphodies-terase was inhibited by low concentrations of cGMP and …

Human insulin–like growth factor I (IGF–I) accumulates in both folded and aggregated forms
in the fermentation medium and cellular periplasmic space when expressed in E. coli with …

Agents such as prostaglandins E1 and I2 which elevate cAMP levels in platelets also increase
cAMP phosphodiesterase activity. Since much of the cAMP phosphodiesterase activity in …

Recombinant DNA techniques were used to biosynthesize human insulin-like growth factor I
(hIGF-I) as a fusion protein wherein the fusion polypeptide is an IgG-binding moiety derived …

During preparative reversed-phase chromatography of recombinant human insulin-like growth
factor-I (IGF), the separation of IGF from IGF aggregates cannot be determined using UV …

A highly selective electrophoretic system employing differential hydrophobic interaction was
evaluated for the quantitative determination of recombinant insulin-like growth factor I (IGF-I) …

… feed efficiency were achieved with a methiIn previous experiments (Reifsnyder, DH,
onine concentration equivalent to 0.51% of Young, CT and Jones, EE, unpublished …

The isolation of recombinant human insulin-like growth factor 1 (rhIGF-1) is complicated by
the presence of several rhIGF-1 variants which co-purify using conventional chromatographic …

Adsorption chromatography using underivatized porous glass can be an effective capture
step for the purification of recombinant proteins. Classical desorption techniques using …