Detail of "6318-55-4"

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Renal specific delivery of sulfamethoxazole in the rat by coupling to the low molecular weight protein lysozyme via an acid-sensitive linker

Renal specific delivery of sulfamethoxazole in the rat by coupling to the low molecular weight protein lysozyme via an acid-sensitive linker. Franssen, Eric J. F.Several substances are used for example 723-46-6 and 6318-55-4 which are their cas registry numbers.; Moolenaar, Frits; De Zeeuw, Dick; Meijer, Dirk K. F. (Dep. Pharmacol. Pharmacother., Univ. Cent. Pharm., Groningen 9713 AW, Neth.). Int. J. Pharm., 80(2-3), R15-R19 (English) 1992. CODEN: IJPHDE. ISSN: 0378-5173. DOCUMENT TYPE: Journal CA Section: 63 (Pharmaceuticals) Section cross-reference(s): 1 Sulfamethoxazole (SM) was converted to a renal specific drug targeting prepn. by coupling the drug to egg-white lysozyme via an acid-sensitive cis-aconityl linker (1:1). Due to this chem. manipulation SM was rapidly distributed to the kidney. Both in vitro and in vivo data indicate that SM was uncoupled from the carrier by chem. hydrolysis in the lysosomes of proximal tubular cells, resulting in parent active drug at the target site. This concept is applicable to other drug-polypeptide conjugates which rapidly distribute to the kidney and might enable selective manipulation of renal (patho)physiol. .

The structure and function of ribonuclease T1

The structure and function of ribonuclease T1. XXIII. Inactivation of ribonuclease T1 by reversible blocking of amino groups with cis-aconitic anhydride and related dicarboxylic acid anhydrides. Takahashi, Kenji (Fac. Sci., Univ. Tokyo, Tokyo, Japan). J. Biochem. (Tokyo), 81(3), 641-6 (English) 1977. CODEN: JOBIAO. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) RNase T1 (I) was inactivated rapidly by treatment at pH 8.0 and 0.degree. with cis-aconitic anhydride (II) and related dicarboxylic acid anhydrides, including citraconic (III), maleic, and succinic (IV) anhydrides. Under the reaction conditions used, approx. 90% inactivation occurred within 30 min. Anal. of inactivated I indicated that the reaction took place rather specifically at the .alpha.-NH2 group of the N-terminal alanine and the .epsilon.-NH2 group of lysine-41. Upon incubation of inactivated I at pH 3.6 and 37.degree., the activity was regenerated to various extents, depending on the nature of the acyl groups introduced. Under these conditions, I modified with II or III recovered much of the original activity after 48 h, whereas I modified with maleic anhydride recovered its activity only partially. Practically no activity was regenerated in the case of I modified with IV under these conditions. The inactivation appears to be due mainly to the effect of the CO2H group introduced at the .epsilon.-NH2 group of lysine-41. 9026-12-4 and 6318-55-4 are just another two chemicals used in this study. The results suggest the usefulness of II as a reversible blocking reagent for NH2 groups in proteins. .