L
Larry R. Krepski
Researcher at 3M
Publications - 101
Citations - 1873
Larry R. Krepski is an academic researcher from 3M. The author has contributed to research in topics: Monomer & Adhesive. The author has an hindex of 23, co-authored 101 publications receiving 1854 citations. Previous affiliations of Larry R. Krepski include Binghamton University & University of Colorado Boulder.
Papers
More filters
Journal ArticleDOI
Aminopyridines as acylation catalysts for tertiary alcohols
Alfred Hassner,Alfred Hassner,Larry R. Krepski,Larry R. Krepski,Vazken Alexanian,Vazken Alexanian +5 more
TL;DR: In this article, a number of 4-substituted pyridines were found to be acylation catalysts, the most effective being 4-pyrrolidinopyridine 4 and 1,1,3,3-tetramethyl-4-(4pyridyl)guanidine 8.
Journal ArticleDOI
Chemistry and technology of 2‐alkenyl azlactones
TL;DR: A chronology of 2-alkenyl azlactone research at 3M is discussed in this paper in terms of its origination; consideration of economics, overall safety, and opportunities for patent protection; elaboration of the chemistry; and applying lessons learned toward the development of commercial technologies.
Journal ArticleDOI
Cycloadditions. 24. An improved procedure for the addition of dichloroketene to unreactive olefins
Larry R. Krepski,Alfred Hassner +1 more
Patent
Azlactone-functional substrates, corneal prostheses, and manufacture and use thereof
TL;DR: Azlactone-functional substrates (especially hydrogels), mammalian body implants, and methods of making and using them are disclosed in this paper, where the authors describe the reaction product of substrates having azlactones-reactive nucleophilic surfaces and a multi-functional azlatone composition having at least two azlatactone moieties.
Journal ArticleDOI
Immobilization of Protein A at high density on azlactone-functional polymeric beads and their use in affinity chromatography
Patrick L. Coleman,Margaret M. Walker,Dean S. Milbrath,Darlene M. Stauffer,Jerald K. Rasmussen,Larry R. Krepski,Steven M. Heilmann +6 more
TL;DR: The results of the use of highly cross-linked, porous, hydrophilic copolymer beads with protein immobilized on their surface for affinity chromatography with marked enhancement in the amount of protein coupled, its rate of reaction, and its biological activity.